Manganese in PDB 6zee: Structure of PP1(7-300) Bound to PHACTR1 (507-580) at PH8.4
Enzymatic activity of Structure of PP1(7-300) Bound to PHACTR1 (507-580) at PH8.4
All present enzymatic activity of Structure of PP1(7-300) Bound to PHACTR1 (507-580) at PH8.4:
3.1.3.16;
Protein crystallography data
The structure of Structure of PP1(7-300) Bound to PHACTR1 (507-580) at PH8.4, PDB code: 6zee
was solved by
S.Mouilleron,
R.Treisman,
R.Fedoryshchak,
R.Lee,
A.M.Butler,
M.Prechova,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
|
Resolution Low / High (Å)
|
119.25 /
1.90
|
|
Space group
|
P 65
|
|
Cell size a, b, c (Å), α, β, γ (°)
|
137.695,
137.695,
238.793,
90.00,
90.00,
120.00
|
|
R / Rfree (%)
|
23.6 /
26.8
|
Manganese Binding Sites:
Pages:
>>> Page 1 <<<
Page 2, Binding sites: 11 -
12;
Binding sites:
The binding sites of Manganese atom in the Structure of PP1(7-300) Bound to PHACTR1 (507-580) at PH8.4
(pdb code 6zee). This binding sites where shown within
5.0 Angstroms radius around Manganese atom.
In total 12 binding sites of Manganese where determined in the
Structure of PP1(7-300) Bound to PHACTR1 (507-580) at PH8.4, PDB code: 6zee:
Jump to Manganese binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
9;
10;
Manganese binding site 1 out
of 12 in 6zee
Go back to
Manganese Binding Sites List in 6zee
Manganese binding site 1 out
of 12 in the Structure of PP1(7-300) Bound to PHACTR1 (507-580) at PH8.4
 Mono view
 Stereo pair view
|
|
A full contact list of Manganese with other atoms in the Mn binding
site number 1 of Structure of PP1(7-300) Bound to PHACTR1 (507-580) at PH8.4 within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
P:Mn501
b:33.8
occ:1.00
|
HD1
|
P:HIS248
|
1.7
|
51.0
|
1.0
|
|
O2
|
P:SO4512
|
2.0
|
39.8
|
1.0
|
|
OD1
|
P:ASP92
|
2.2
|
36.7
|
1.0
|
|
OD1
|
P:ASN124
|
2.2
|
39.5
|
1.0
|
|
NE2
|
P:HIS173
|
2.3
|
37.1
|
1.0
|
|
ND1
|
P:HIS248
|
2.5
|
42.4
|
1.0
|
|
HE1
|
P:HIS248
|
2.9
|
52.6
|
1.0
|
|
CE1
|
P:HIS248
|
3.0
|
43.7
|
1.0
|
|
HD21
|
P:ASN124
|
3.0
|
46.6
|
1.0
|
|
MN
|
P:MN502
|
3.1
|
43.7
|
1.0
|
|
HA
|
P:HIS248
|
3.1
|
53.7
|
1.0
|
|
CE1
|
P:HIS173
|
3.1
|
37.3
|
1.0
|
|
CG
|
P:ASN124
|
3.2
|
38.4
|
1.0
|
|
S
|
P:SO4512
|
3.3
|
42.4
|
1.0
|
|
CG
|
P:ASP92
|
3.3
|
37.1
|
1.0
|
|
HE1
|
P:HIS173
|
3.3
|
44.9
|
1.0
|
|
HD2
|
P:HIS125
|
3.3
|
46.9
|
1.0
|
|
CD2
|
P:HIS173
|
3.3
|
38.7
|
1.0
|
|
ND2
|
P:ASN124
|
3.5
|
39.0
|
1.0
|
|
O1
|
P:SO4512
|
3.5
|
49.8
|
1.0
|
|
HD2
|
P:HIS173
|
3.5
|
46.6
|
1.0
|
|
OD2
|
P:ASP92
|
3.7
|
36.9
|
1.0
|
|
CG
|
P:HIS248
|
3.7
|
42.3
|
1.0
|
|
O4
|
P:SO4512
|
3.9
|
42.9
|
1.0
|
|
H
|
P:ASN124
|
4.0
|
43.9
|
1.0
|
|
OD2
|
P:ASP64
|
4.0
|
39.1
|
1.0
|
|
CA
|
P:HIS248
|
4.0
|
44.6
|
1.0
|
|
CD2
|
P:HIS125
|
4.1
|
38.9
|
1.0
|
|
O
|
P:HIS248
|
4.2
|
45.1
|
1.0
|
|
NE2
|
P:HIS248
|
4.3
|
43.1
|
1.0
|
|
HE2
|
P:HIS125
|
4.3
|
47.0
|
1.0
|
|
ND1
|
P:HIS173
|
4.3
|
36.1
|
1.0
|
|
HD22
|
P:ASN124
|
4.3
|
46.6
|
1.0
|
|
CB
|
P:HIS248
|
4.3
|
41.7
|
1.0
|
|
O3
|
P:SO4512
|
4.4
|
38.1
|
1.0
|
|
HH12
|
P:ARG221
|
4.4
|
51.9
|
1.0
|
|
CG
|
P:HIS173
|
4.4
|
36.6
|
1.0
|
|
HB2
|
P:HIS248
|
4.5
|
50.2
|
1.0
|
|
CB
|
P:ASP92
|
4.5
|
35.5
|
1.0
|
|
CB
|
P:ASN124
|
4.5
|
39.0
|
1.0
|
|
NE2
|
P:HIS125
|
4.6
|
39.0
|
1.0
|
|
HB2
|
P:ASP92
|
4.6
|
42.5
|
1.0
|
|
C
|
P:HIS248
|
4.6
|
43.5
|
1.0
|
|
CD2
|
P:HIS248
|
4.6
|
43.4
|
1.0
|
|
N
|
P:ASN124
|
4.7
|
37.2
|
1.0
|
|
HB3
|
P:ASN124
|
4.7
|
47.0
|
1.0
|
|
NH1
|
P:ARG221
|
4.8
|
43.2
|
1.0
|
|
HB3
|
P:ASP92
|
4.8
|
42.5
|
1.0
|
|
HE1
|
P:HIS66
|
4.8
|
48.0
|
1.0
|
|
NE2
|
P:HIS66
|
4.8
|
41.1
|
1.0
|
|
H
|
P:HIS125
|
4.8
|
43.8
|
1.0
|
|
O
|
P:LEU205
|
4.8
|
41.3
|
1.0
|
|
HH22
|
P:ARG221
|
4.9
|
52.1
|
1.0
|
|
HE2
|
P:HIS248
|
4.9
|
51.9
|
1.0
|
|
H
|
P:HIS248
|
5.0
|
47.4
|
1.0
|
|
Manganese binding site 2 out
of 12 in 6zee
Go back to
Manganese Binding Sites List in 6zee
Manganese binding site 2 out
of 12 in the Structure of PP1(7-300) Bound to PHACTR1 (507-580) at PH8.4
 Mono view
 Stereo pair view
|
|
A full contact list of Manganese with other atoms in the Mn binding
site number 2 of Structure of PP1(7-300) Bound to PHACTR1 (507-580) at PH8.4 within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
P:Mn502
b:43.7
occ:1.00
|
O1
|
P:SO4512
|
2.1
|
49.8
|
1.0
|
|
NE2
|
P:HIS66
|
2.1
|
41.1
|
1.0
|
|
OD1
|
P:ASP92
|
2.4
|
36.7
|
1.0
|
|
OD2
|
P:ASP64
|
2.4
|
39.1
|
1.0
|
|
O
|
P:HOH623
|
2.5
|
40.8
|
1.0
|
|
CE1
|
P:HIS66
|
2.9
|
39.9
|
1.0
|
|
HE1
|
P:HIS66
|
3.0
|
48.0
|
1.0
|
|
MN
|
P:MN501
|
3.1
|
33.8
|
1.0
|
|
S
|
P:SO4512
|
3.2
|
42.4
|
1.0
|
|
CD2
|
P:HIS66
|
3.2
|
37.6
|
1.0
|
|
O2
|
P:SO4512
|
3.3
|
39.8
|
1.0
|
|
HH22
|
P:ARG96
|
3.3
|
54.7
|
1.0
|
|
CG
|
P:ASP92
|
3.3
|
37.1
|
1.0
|
|
HB3
|
P:ASP92
|
3.4
|
42.5
|
1.0
|
|
HD2
|
P:HIS66
|
3.4
|
45.2
|
1.0
|
|
CG
|
P:ASP64
|
3.6
|
37.1
|
1.0
|
|
HD2
|
P:HIS125
|
3.8
|
46.9
|
1.0
|
|
CB
|
P:ASP92
|
3.8
|
35.5
|
1.0
|
|
HE1
|
P:HIS173
|
3.8
|
44.9
|
1.0
|
|
HH21
|
P:ARG96
|
3.9
|
54.7
|
1.0
|
|
HB3
|
P:ASP64
|
3.9
|
44.8
|
1.0
|
|
HB2
|
P:ASP92
|
3.9
|
42.5
|
1.0
|
|
NH2
|
P:ARG96
|
3.9
|
45.5
|
1.0
|
|
O4
|
P:SO4512
|
3.9
|
42.9
|
1.0
|
|
HH
|
P:TYR272
|
4.0
|
50.6
|
1.0
|
|
HE2
|
P:HIS125
|
4.0
|
47.0
|
1.0
|
|
O
|
P:HOH667
|
4.1
|
42.0
|
1.0
|
|
HA
|
P:HIS248
|
4.1
|
53.7
|
1.0
|
|
ND1
|
P:HIS66
|
4.1
|
40.1
|
1.0
|
|
HD1
|
P:HIS248
|
4.1
|
51.0
|
1.0
|
|
HE1
|
P:PHE267
|
4.1
|
46.0
|
1.0
|
|
CD2
|
P:HIS125
|
4.1
|
38.9
|
1.0
|
|
CG
|
P:HIS66
|
4.2
|
37.6
|
1.0
|
|
NE2
|
P:HIS125
|
4.3
|
39.0
|
1.0
|
|
OH
|
P:TYR272
|
4.3
|
42.0
|
1.0
|
|
O3
|
P:SO4512
|
4.3
|
38.1
|
1.0
|
|
CB
|
P:ASP64
|
4.3
|
37.2
|
1.0
|
|
OD2
|
P:ASP92
|
4.4
|
36.9
|
1.0
|
|
CE1
|
P:HIS173
|
4.4
|
37.3
|
1.0
|
|
NE2
|
P:HIS173
|
4.4
|
37.1
|
1.0
|
|
OD1
|
P:ASP64
|
4.6
|
35.7
|
1.0
|
|
O
|
P:HIS248
|
4.6
|
45.1
|
1.0
|
|
HB2
|
P:ASP64
|
4.7
|
44.8
|
1.0
|
|
OD1
|
P:ASN124
|
4.8
|
39.5
|
1.0
|
|
HD1
|
P:HIS66
|
4.9
|
48.3
|
1.0
|
|
ND1
|
P:HIS248
|
4.9
|
42.4
|
1.0
|
|
CA
|
P:HIS248
|
5.0
|
44.6
|
1.0
|
|
CE1
|
P:PHE267
|
5.0
|
38.5
|
1.0
|
|
HD21
|
P:ASN124
|
5.0
|
46.6
|
1.0
|
|
Manganese binding site 3 out
of 12 in 6zee
Go back to
Manganese Binding Sites List in 6zee
Manganese binding site 3 out
of 12 in the Structure of PP1(7-300) Bound to PHACTR1 (507-580) at PH8.4
 Mono view
 Stereo pair view
|
|
A full contact list of Manganese with other atoms in the Mn binding
site number 3 of Structure of PP1(7-300) Bound to PHACTR1 (507-580) at PH8.4 within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
Q:Mn501
b:39.5
occ:1.00
|
OD1
|
Q:ASN124
|
2.2
|
48.4
|
1.0
|
|
NE2
|
Q:HIS173
|
2.2
|
46.4
|
1.0
|
|
OD2
|
Q:ASP92
|
2.3
|
49.9
|
1.0
|
|
O4
|
Q:SO4508
|
2.4
|
44.5
|
1.0
|
|
ND1
|
Q:HIS248
|
2.5
|
44.3
|
1.0
|
|
O
|
Q:HOH601
|
2.5
|
46.2
|
1.0
|
|
HE1
|
Q:HIS248
|
2.8
|
51.4
|
1.0
|
|
CE1
|
Q:HIS248
|
3.0
|
42.7
|
1.0
|
|
MN
|
Q:MN502
|
3.0
|
49.1
|
1.0
|
|
CE1
|
Q:HIS173
|
3.1
|
43.6
|
1.0
|
|
HA
|
Q:HIS248
|
3.1
|
51.7
|
1.0
|
|
HD21
|
Q:ASN124
|
3.1
|
56.6
|
1.0
|
|
CG
|
Q:ASN124
|
3.2
|
48.0
|
1.0
|
|
CG
|
Q:ASP92
|
3.2
|
50.1
|
1.0
|
|
HE1
|
Q:HIS173
|
3.2
|
52.5
|
1.0
|
|
CD2
|
Q:HIS173
|
3.3
|
45.5
|
1.0
|
|
HD2
|
Q:HIS125
|
3.3
|
58.7
|
1.0
|
|
S
|
Q:SO4508
|
3.4
|
42.6
|
1.0
|
|
HD2
|
Q:HIS173
|
3.5
|
54.8
|
1.0
|
|
ND2
|
Q:ASN124
|
3.5
|
47.8
|
1.0
|
|
OD1
|
Q:ASP92
|
3.5
|
49.8
|
1.0
|
|
O1
|
Q:SO4508
|
3.6
|
49.0
|
1.0
|
|
CG
|
Q:HIS248
|
3.7
|
42.8
|
1.0
|
|
O2
|
Q:SO4508
|
3.7
|
40.4
|
1.0
|
|
H
|
Q:ASN124
|
3.9
|
57.3
|
1.0
|
|
CA
|
Q:HIS248
|
4.0
|
43.0
|
1.0
|
|
CD2
|
Q:HIS125
|
4.1
|
49.6
|
1.0
|
|
OD2
|
Q:ASP64
|
4.2
|
47.6
|
1.0
|
|
NE2
|
Q:HIS248
|
4.3
|
41.3
|
1.0
|
|
ND1
|
Q:HIS173
|
4.3
|
43.6
|
1.0
|
|
O
|
Q:HIS248
|
4.3
|
46.8
|
1.0
|
|
CB
|
Q:HIS248
|
4.3
|
41.6
|
1.0
|
|
HE2
|
Q:HIS125
|
4.4
|
58.8
|
1.0
|
|
CG
|
Q:HIS173
|
4.4
|
43.3
|
1.0
|
|
HD22
|
Q:ASN124
|
4.4
|
56.6
|
1.0
|
|
CB
|
Q:ASP92
|
4.5
|
50.9
|
1.0
|
|
HB2
|
Q:HIS248
|
4.5
|
50.1
|
1.0
|
|
HB2
|
Q:ASP92
|
4.5
|
60.2
|
1.0
|
|
CB
|
Q:ASN124
|
4.5
|
47.6
|
1.0
|
|
HH12
|
Q:ARG221
|
4.5
|
48.6
|
1.0
|
|
CD2
|
Q:HIS248
|
4.6
|
40.4
|
1.0
|
|
NE2
|
Q:HIS125
|
4.6
|
49.5
|
1.0
|
|
O3
|
Q:SO4508
|
4.6
|
44.0
|
1.0
|
|
N
|
Q:ASN124
|
4.7
|
48.4
|
1.0
|
|
HB3
|
Q:ASN124
|
4.7
|
56.3
|
1.0
|
|
C
|
Q:HIS248
|
4.7
|
44.9
|
1.0
|
|
O
|
Q:LEU205
|
4.7
|
42.1
|
1.0
|
|
HB3
|
Q:ASP92
|
4.8
|
60.2
|
1.0
|
|
H
|
Q:HIS125
|
4.8
|
58.1
|
1.0
|
|
HE1
|
Q:HIS66
|
4.8
|
56.6
|
1.0
|
|
NE2
|
Q:HIS66
|
4.8
|
49.6
|
1.0
|
|
HE2
|
Q:HIS248
|
4.9
|
49.7
|
1.0
|
|
H
|
Q:HIS248
|
4.9
|
52.6
|
1.0
|
|
NH1
|
Q:ARG221
|
5.0
|
40.4
|
1.0
|
|
Manganese binding site 4 out
of 12 in 6zee
Go back to
Manganese Binding Sites List in 6zee
Manganese binding site 4 out
of 12 in the Structure of PP1(7-300) Bound to PHACTR1 (507-580) at PH8.4
 Mono view
 Stereo pair view
|
|
A full contact list of Manganese with other atoms in the Mn binding
site number 4 of Structure of PP1(7-300) Bound to PHACTR1 (507-580) at PH8.4 within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
Q:Mn502
b:49.1
occ:1.00
|
NE2
|
Q:HIS66
|
2.0
|
49.6
|
1.0
|
|
OD2
|
Q:ASP92
|
2.1
|
49.9
|
1.0
|
|
O1
|
Q:SO4508
|
2.2
|
49.0
|
1.0
|
|
OD2
|
Q:ASP64
|
2.5
|
47.6
|
1.0
|
|
O
|
Q:HOH601
|
2.7
|
46.2
|
1.0
|
|
CE1
|
Q:HIS66
|
2.9
|
47.0
|
1.0
|
|
HE1
|
Q:HIS66
|
3.0
|
56.6
|
1.0
|
|
MN
|
Q:MN501
|
3.0
|
39.5
|
1.0
|
|
CD2
|
Q:HIS66
|
3.2
|
47.4
|
1.0
|
|
S
|
Q:SO4508
|
3.2
|
42.6
|
1.0
|
|
CG
|
Q:ASP92
|
3.2
|
50.1
|
1.0
|
|
HB3
|
Q:ASP92
|
3.3
|
60.2
|
1.0
|
|
HD2
|
Q:HIS66
|
3.4
|
57.1
|
1.0
|
|
O4
|
Q:SO4508
|
3.4
|
44.5
|
1.0
|
|
O2
|
Q:SO4508
|
3.6
|
40.4
|
1.0
|
|
CG
|
Q:ASP64
|
3.7
|
45.7
|
1.0
|
|
CB
|
Q:ASP92
|
3.7
|
50.9
|
1.0
|
|
HD2
|
Q:HIS125
|
3.7
|
58.7
|
1.0
|
|
HE1
|
Q:HIS173
|
3.7
|
52.5
|
1.0
|
|
HB2
|
Q:ASP92
|
3.8
|
60.2
|
1.0
|
|
HB3
|
Q:ASP64
|
3.9
|
57.2
|
1.0
|
|
HE2
|
Q:HIS125
|
4.0
|
58.8
|
1.0
|
|
HA
|
Q:HIS248
|
4.0
|
51.7
|
1.0
|
|
ND1
|
Q:HIS66
|
4.1
|
52.3
|
1.0
|
|
CD2
|
Q:HIS125
|
4.1
|
49.6
|
1.0
|
|
HE
|
Q:ARG96
|
4.2
|
68.1
|
1.0
|
|
HE1
|
Q:PHE267
|
4.2
|
53.7
|
1.0
|
|
CG
|
Q:HIS66
|
4.2
|
47.3
|
1.0
|
|
NE2
|
Q:HIS125
|
4.2
|
49.5
|
1.0
|
|
HH
|
Q:TYR272
|
4.3
|
62.9
|
1.0
|
|
OH
|
Q:TYR272
|
4.3
|
53.0
|
1.0
|
|
OD1
|
Q:ASP92
|
4.3
|
49.8
|
1.0
|
|
CB
|
Q:ASP64
|
4.3
|
47.5
|
1.0
|
|
NE2
|
Q:HIS173
|
4.4
|
46.4
|
1.0
|
|
CE1
|
Q:HIS173
|
4.4
|
43.6
|
1.0
|
|
O
|
Q:HOH649
|
4.4
|
45.3
|
1.0
|
|
O3
|
Q:SO4508
|
4.5
|
44.0
|
1.0
|
|
O
|
Q:HIS248
|
4.5
|
46.8
|
1.0
|
|
OD1
|
Q:ASP64
|
4.6
|
44.2
|
1.0
|
|
OD1
|
Q:ASN124
|
4.7
|
48.4
|
1.0
|
|
HB2
|
Q:ASP64
|
4.8
|
57.2
|
1.0
|
|
HD1
|
Q:HIS66
|
4.8
|
62.9
|
1.0
|
|
ND1
|
Q:HIS248
|
4.8
|
44.3
|
1.0
|
|
CA
|
Q:HIS248
|
4.9
|
43.0
|
1.0
|
|
HH21
|
Q:ARG96
|
5.0
|
65.6
|
1.0
|
|
C
|
Q:HIS248
|
5.0
|
44.9
|
1.0
|
|
Manganese binding site 5 out
of 12 in 6zee
Go back to
Manganese Binding Sites List in 6zee
Manganese binding site 5 out
of 12 in the Structure of PP1(7-300) Bound to PHACTR1 (507-580) at PH8.4
 Mono view
 Stereo pair view
|
|
A full contact list of Manganese with other atoms in the Mn binding
site number 5 of Structure of PP1(7-300) Bound to PHACTR1 (507-580) at PH8.4 within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mn501
b:36.2
occ:1.00
|
O1
|
B:SO4516
|
2.2
|
28.4
|
1.0
|
|
O
|
B:HOH632
|
2.2
|
27.4
|
1.0
|
|
OD1
|
B:ASN124
|
2.2
|
26.1
|
1.0
|
|
OD1
|
B:ASP92
|
2.3
|
25.9
|
1.0
|
|
NE2
|
B:HIS173
|
2.3
|
25.9
|
1.0
|
|
ND1
|
B:HIS248
|
2.4
|
26.9
|
1.0
|
|
HE1
|
B:HIS248
|
2.8
|
33.0
|
1.0
|
|
CE1
|
B:HIS248
|
2.9
|
27.4
|
1.0
|
|
HA
|
B:HIS248
|
3.0
|
32.5
|
1.0
|
|
MN
|
B:MN502
|
3.1
|
37.8
|
1.0
|
|
HD21
|
B:ASN124
|
3.1
|
30.6
|
1.0
|
|
CG
|
B:ASN124
|
3.1
|
25.9
|
1.0
|
|
CG
|
B:ASP92
|
3.2
|
26.8
|
1.0
|
|
CE1
|
B:HIS173
|
3.2
|
25.7
|
1.0
|
|
CD2
|
B:HIS173
|
3.3
|
25.7
|
1.0
|
|
S
|
B:SO4516
|
3.3
|
32.6
|
1.0
|
|
HE1
|
B:HIS173
|
3.4
|
31.0
|
1.0
|
|
HD2
|
B:HIS125
|
3.5
|
32.8
|
1.0
|
|
HD2
|
B:HIS173
|
3.5
|
31.0
|
1.0
|
|
ND2
|
B:ASN124
|
3.5
|
25.3
|
1.0
|
|
OD2
|
B:ASP92
|
3.5
|
23.5
|
1.0
|
|
O2
|
B:SO4516
|
3.6
|
31.4
|
1.0
|
|
CG
|
B:HIS248
|
3.6
|
26.4
|
1.0
|
|
O4
|
B:SO4516
|
3.9
|
31.8
|
1.0
|
|
H
|
B:ASN124
|
3.9
|
29.9
|
1.0
|
|
CA
|
B:HIS248
|
3.9
|
26.9
|
1.0
|
|
OD2
|
B:ASP64
|
4.0
|
26.8
|
1.0
|
|
O
|
B:HIS248
|
4.1
|
29.6
|
1.0
|
|
NE2
|
B:HIS248
|
4.2
|
26.4
|
1.0
|
|
CB
|
B:HIS248
|
4.2
|
26.4
|
1.0
|
|
CD2
|
B:HIS125
|
4.3
|
27.2
|
1.0
|
|
HD22
|
B:ASN124
|
4.3
|
30.6
|
1.0
|
|
ND1
|
B:HIS173
|
4.4
|
25.2
|
1.0
|
|
HB2
|
B:HIS248
|
4.4
|
31.9
|
1.0
|
|
CB
|
B:ASP92
|
4.4
|
24.9
|
1.0
|
|
CG
|
B:HIS173
|
4.5
|
24.9
|
1.0
|
|
HB2
|
B:ASP92
|
4.5
|
30.0
|
1.0
|
|
C
|
B:HIS248
|
4.5
|
28.3
|
1.0
|
|
CB
|
B:ASN124
|
4.5
|
25.9
|
1.0
|
|
O3
|
B:SO4516
|
4.5
|
31.4
|
1.0
|
|
CD2
|
B:HIS248
|
4.5
|
26.9
|
1.0
|
|
HH12
|
B:ARG221
|
4.5
|
37.2
|
1.0
|
|
N
|
B:ASN124
|
4.6
|
24.8
|
1.0
|
|
HB3
|
B:ASN124
|
4.7
|
31.2
|
1.0
|
|
HE2
|
B:HIS125
|
4.7
|
32.9
|
1.0
|
|
HB3
|
B:ASP92
|
4.8
|
30.0
|
1.0
|
|
H
|
B:HIS125
|
4.8
|
31.2
|
1.0
|
|
O
|
B:LEU205
|
4.8
|
24.9
|
1.0
|
|
HE1
|
B:HIS66
|
4.8
|
36.4
|
1.0
|
|
NE2
|
B:HIS66
|
4.8
|
30.1
|
1.0
|
|
HE2
|
B:HIS248
|
4.9
|
31.8
|
1.0
|
|
H
|
B:HIS248
|
4.9
|
31.6
|
1.0
|
|
N
|
B:HIS248
|
4.9
|
26.2
|
1.0
|
|
NE2
|
B:HIS125
|
5.0
|
27.3
|
1.0
|
|
CG
|
B:ASP64
|
5.0
|
27.3
|
1.0
|
|
NH1
|
B:ARG221
|
5.0
|
30.9
|
1.0
|
|
O
|
B:HOH644
|
5.0
|
31.5
|
1.0
|
|
Manganese binding site 6 out
of 12 in 6zee
Go back to
Manganese Binding Sites List in 6zee
Manganese binding site 6 out
of 12 in the Structure of PP1(7-300) Bound to PHACTR1 (507-580) at PH8.4
 Mono view
 Stereo pair view
|
|
A full contact list of Manganese with other atoms in the Mn binding
site number 6 of Structure of PP1(7-300) Bound to PHACTR1 (507-580) at PH8.4 within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mn502
b:37.8
occ:1.00
|
O
|
B:HOH632
|
1.9
|
27.4
|
1.0
|
|
NE2
|
B:HIS66
|
2.0
|
30.1
|
1.0
|
|
OD1
|
B:ASP92
|
2.1
|
25.9
|
1.0
|
|
OD2
|
B:ASP64
|
2.2
|
26.8
|
1.0
|
|
O2
|
B:SO4516
|
2.2
|
31.4
|
1.0
|
|
O
|
B:HOH644
|
2.3
|
31.5
|
1.0
|
|
CE1
|
B:HIS66
|
2.9
|
30.2
|
1.0
|
|
HE1
|
B:HIS66
|
3.0
|
36.4
|
1.0
|
|
CD2
|
B:HIS66
|
3.1
|
31.0
|
1.0
|
|
MN
|
B:MN501
|
3.1
|
36.2
|
1.0
|
|
CG
|
B:ASP92
|
3.2
|
26.8
|
1.0
|
|
S
|
B:SO4516
|
3.3
|
32.6
|
1.0
|
|
HB3
|
B:ASP92
|
3.3
|
30.0
|
1.0
|
|
HD2
|
B:HIS66
|
3.3
|
37.3
|
1.0
|
|
O1
|
B:SO4516
|
3.4
|
28.4
|
1.0
|
|
CG
|
B:ASP64
|
3.4
|
27.3
|
1.0
|
|
HH12
|
B:ARG96
|
3.5
|
39.8
|
0.5
|
|
CB
|
B:ASP92
|
3.7
|
24.9
|
1.0
|
|
O4
|
B:SO4516
|
3.8
|
31.8
|
1.0
|
|
HB2
|
B:ASP92
|
3.8
|
30.0
|
1.0
|
|
HB3
|
B:ASP64
|
4.0
|
33.1
|
1.0
|
|
HE1
|
B:HIS173
|
4.0
|
31.0
|
1.0
|
|
HA
|
B:HIS248
|
4.0
|
32.5
|
1.0
|
|
O
|
B:HOH670
|
4.0
|
37.6
|
1.0
|
|
HE2
|
B:PHE267
|
4.0
|
33.5
|
1.0
|
|
HD2
|
B:HIS125
|
4.0
|
32.8
|
1.0
|
|
ND1
|
B:HIS66
|
4.1
|
29.9
|
1.0
|
|
NH1
|
B:ARG96
|
4.1
|
33.0
|
0.5
|
|
HH11
|
B:ARG96
|
4.1
|
39.8
|
0.5
|
|
CG
|
B:HIS66
|
4.2
|
30.2
|
1.0
|
|
OD1
|
B:ASP64
|
4.3
|
26.3
|
1.0
|
|
OD2
|
B:ASP92
|
4.3
|
23.5
|
1.0
|
|
CB
|
B:ASP64
|
4.3
|
27.5
|
1.0
|
|
OH
|
B:TYR272
|
4.3
|
34.3
|
1.0
|
|
O
|
B:HIS248
|
4.4
|
29.6
|
1.0
|
|
CD2
|
B:HIS125
|
4.4
|
27.2
|
1.0
|
|
HE
|
B:ARG96
|
4.5
|
41.0
|
0.5
|
|
HH
|
B:TYR272
|
4.5
|
41.3
|
1.0
|
|
NE2
|
B:HIS173
|
4.5
|
25.9
|
1.0
|
|
O3
|
B:SO4516
|
4.5
|
31.4
|
1.0
|
|
HE2
|
B:HIS125
|
4.5
|
32.9
|
1.0
|
|
CE1
|
B:HIS173
|
4.6
|
25.7
|
1.0
|
|
NE2
|
B:HIS125
|
4.7
|
27.3
|
1.0
|
|
HB2
|
B:ASP64
|
4.7
|
33.1
|
1.0
|
|
OD1
|
B:ASN124
|
4.8
|
26.1
|
1.0
|
|
CE2
|
B:PHE267
|
4.8
|
27.8
|
1.0
|
|
HD1
|
B:HIS66
|
4.8
|
36.1
|
1.0
|
|
CA
|
B:HIS248
|
4.8
|
26.9
|
1.0
|
|
ND1
|
B:HIS248
|
4.8
|
26.9
|
1.0
|
|
C
|
B:HIS248
|
4.9
|
28.3
|
1.0
|
|
HZ
|
B:PHE267
|
4.9
|
34.5
|
1.0
|
|
Manganese binding site 7 out
of 12 in 6zee
Go back to
Manganese Binding Sites List in 6zee
Manganese binding site 7 out
of 12 in the Structure of PP1(7-300) Bound to PHACTR1 (507-580) at PH8.4
 Mono view
 Stereo pair view
|
|
A full contact list of Manganese with other atoms in the Mn binding
site number 7 of Structure of PP1(7-300) Bound to PHACTR1 (507-580) at PH8.4 within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mn501
b:33.6
occ:1.00
|
O
|
A:HOH604
|
1.9
|
32.0
|
1.0
|
|
O4
|
A:SO4518
|
2.1
|
32.6
|
1.0
|
|
NE2
|
A:HIS173
|
2.2
|
26.9
|
1.0
|
|
OD1
|
A:ASN124
|
2.2
|
27.1
|
1.0
|
|
OD2
|
A:ASP92
|
2.2
|
27.1
|
1.0
|
|
ND1
|
A:HIS248
|
2.3
|
28.5
|
1.0
|
|
HE1
|
A:HIS248
|
2.8
|
34.2
|
1.0
|
|
CE1
|
A:HIS248
|
2.9
|
28.4
|
1.0
|
|
HA
|
A:HIS248
|
3.0
|
34.7
|
1.0
|
|
HD21
|
A:ASN124
|
3.1
|
31.8
|
1.0
|
|
CD2
|
A:HIS173
|
3.1
|
26.0
|
1.0
|
|
MN
|
A:MN502
|
3.2
|
37.4
|
1.0
|
|
CG
|
A:ASP92
|
3.2
|
26.8
|
1.0
|
|
CE1
|
A:HIS173
|
3.2
|
26.8
|
1.0
|
|
CG
|
A:ASN124
|
3.2
|
26.2
|
1.0
|
|
HD2
|
A:HIS173
|
3.3
|
31.4
|
1.0
|
|
HE1
|
A:HIS173
|
3.4
|
32.3
|
1.0
|
|
HD2
|
A:HIS125
|
3.4
|
33.6
|
1.0
|
|
S
|
A:SO4518
|
3.4
|
35.8
|
1.0
|
|
ND2
|
A:ASN124
|
3.5
|
26.3
|
1.0
|
|
OD1
|
A:ASP92
|
3.5
|
26.2
|
1.0
|
|
CG
|
A:HIS248
|
3.5
|
27.9
|
1.0
|
|
O3
|
A:SO4518
|
3.8
|
32.7
|
1.0
|
|
H
|
A:ASN124
|
3.9
|
31.1
|
1.0
|
|
CA
|
A:HIS248
|
3.9
|
28.8
|
1.0
|
|
OD2
|
A:ASP64
|
4.0
|
29.4
|
1.0
|
|
O2
|
A:SO4518
|
4.1
|
34.9
|
1.0
|
|
CB
|
A:HIS248
|
4.1
|
27.4
|
1.0
|
|
O
|
A:HIS248
|
4.1
|
32.2
|
1.0
|
|
NE2
|
A:HIS248
|
4.2
|
27.2
|
1.0
|
|
CD2
|
A:HIS125
|
4.2
|
27.9
|
1.0
|
|
ND1
|
A:HIS173
|
4.3
|
26.0
|
1.0
|
|
HB2
|
A:HIS248
|
4.3
|
33.1
|
1.0
|
|
CG
|
A:HIS173
|
4.3
|
25.6
|
1.0
|
|
HD22
|
A:ASN124
|
4.4
|
31.8
|
1.0
|
|
O1
|
A:SO4518
|
4.4
|
33.4
|
1.0
|
|
CB
|
A:ASP92
|
4.5
|
25.1
|
1.0
|
|
CD2
|
A:HIS248
|
4.5
|
27.7
|
1.0
|
|
HH12
|
A:ARG221
|
4.5
|
36.5
|
1.0
|
|
HB2
|
A:ASP92
|
4.5
|
30.2
|
1.0
|
|
C
|
A:HIS248
|
4.5
|
30.5
|
1.0
|
|
CB
|
A:ASN124
|
4.6
|
26.0
|
1.0
|
|
N
|
A:ASN124
|
4.6
|
25.8
|
1.0
|
|
HE2
|
A:HIS125
|
4.6
|
36.1
|
1.0
|
|
H
|
A:HIS125
|
4.7
|
29.4
|
1.0
|
|
O
|
A:LEU205
|
4.7
|
24.6
|
1.0
|
|
HB3
|
A:ASP92
|
4.8
|
30.2
|
1.0
|
|
HB3
|
A:ASN124
|
4.8
|
31.3
|
1.0
|
|
H
|
A:HIS248
|
4.8
|
31.9
|
1.0
|
|
HE2
|
A:HIS248
|
4.8
|
32.8
|
1.0
|
|
NE2
|
A:HIS125
|
4.8
|
29.9
|
1.0
|
|
N
|
A:HIS248
|
4.9
|
26.5
|
1.0
|
|
NH1
|
A:ARG221
|
4.9
|
30.3
|
1.0
|
|
HH22
|
A:ARG221
|
4.9
|
36.7
|
1.0
|
|
HE1
|
A:HIS66
|
5.0
|
35.2
|
1.0
|
|
NE2
|
A:HIS66
|
5.0
|
30.0
|
1.0
|
|
Manganese binding site 8 out
of 12 in 6zee
Go back to
Manganese Binding Sites List in 6zee
Manganese binding site 8 out
of 12 in the Structure of PP1(7-300) Bound to PHACTR1 (507-580) at PH8.4
 Mono view
 Stereo pair view
|
|
A full contact list of Manganese with other atoms in the Mn binding
site number 8 of Structure of PP1(7-300) Bound to PHACTR1 (507-580) at PH8.4 within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mn502
b:37.4
occ:1.00
|
OD2
|
A:ASP64
|
2.1
|
29.4
|
1.0
|
|
NE2
|
A:HIS66
|
2.1
|
30.0
|
1.0
|
|
O
|
A:HOH604
|
2.2
|
32.0
|
1.0
|
|
OD2
|
A:ASP92
|
2.2
|
27.1
|
1.0
|
|
O3
|
A:SO4518
|
2.3
|
32.7
|
1.0
|
|
O
|
A:HOH606
|
2.4
|
32.4
|
1.0
|
|
CE1
|
A:HIS66
|
3.1
|
29.2
|
1.0
|
|
HO1
|
A:EDO508
|
3.1
|
50.2
|
1.0
|
|
CD2
|
A:HIS66
|
3.2
|
28.7
|
1.0
|
|
MN
|
A:MN501
|
3.2
|
33.6
|
1.0
|
|
O4
|
A:SO4518
|
3.2
|
32.6
|
1.0
|
|
HE1
|
A:HIS66
|
3.2
|
35.2
|
1.0
|
|
CG
|
A:ASP92
|
3.3
|
26.8
|
1.0
|
|
S
|
A:SO4518
|
3.3
|
35.8
|
1.0
|
|
HB3
|
A:ASP92
|
3.3
|
30.2
|
1.0
|
|
HD2
|
A:HIS66
|
3.3
|
34.5
|
1.0
|
|
CG
|
A:ASP64
|
3.4
|
28.6
|
1.0
|
|
CB
|
A:ASP92
|
3.7
|
25.1
|
1.0
|
|
HB2
|
A:ASP92
|
3.8
|
30.2
|
1.0
|
|
HB3
|
A:ASP64
|
3.8
|
35.4
|
1.0
|
|
HE1
|
A:HIS173
|
3.8
|
32.3
|
1.0
|
|
HE1
|
A:PHE267
|
3.9
|
37.1
|
1.0
|
|
O2
|
A:SO4518
|
3.9
|
34.9
|
1.0
|
|
HA
|
A:HIS248
|
3.9
|
34.7
|
1.0
|
|
HD2
|
A:HIS125
|
4.0
|
33.6
|
1.0
|
|
O1
|
A:EDO508
|
4.1
|
41.7
|
1.0
|
|
CB
|
A:ASP64
|
4.2
|
29.4
|
1.0
|
|
ND1
|
A:HIS66
|
4.2
|
30.2
|
1.0
|
|
CG
|
A:HIS66
|
4.3
|
28.4
|
1.0
|
|
OD1
|
A:ASP64
|
4.3
|
27.2
|
1.0
|
|
NE2
|
A:HIS173
|
4.3
|
26.9
|
1.0
|
|
HE
|
A:ARG96
|
4.3
|
48.7
|
1.0
|
|
OD1
|
A:ASP92
|
4.4
|
26.2
|
1.0
|
|
H12
|
A:EDO508
|
4.4
|
44.2
|
1.0
|
|
CE1
|
A:HIS173
|
4.4
|
26.8
|
1.0
|
|
CD2
|
A:HIS125
|
4.4
|
27.9
|
1.0
|
|
O
|
A:HIS248
|
4.4
|
32.2
|
1.0
|
|
OH
|
A:TYR272
|
4.5
|
34.7
|
1.0
|
|
HE2
|
A:HIS125
|
4.5
|
36.1
|
1.0
|
|
O1
|
A:SO4518
|
4.5
|
33.4
|
1.0
|
|
H11
|
A:EDO508
|
4.5
|
44.2
|
1.0
|
|
C1
|
A:EDO508
|
4.6
|
36.7
|
1.0
|
|
HB2
|
A:ASP64
|
4.6
|
35.4
|
1.0
|
|
HH
|
A:TYR272
|
4.6
|
41.8
|
1.0
|
|
NE2
|
A:HIS125
|
4.6
|
29.9
|
1.0
|
|
CE1
|
A:PHE267
|
4.7
|
30.8
|
1.0
|
|
CA
|
A:HIS248
|
4.8
|
28.8
|
1.0
|
|
C
|
A:HIS248
|
4.9
|
30.5
|
1.0
|
|
ND1
|
A:HIS248
|
4.9
|
28.5
|
1.0
|
|
H
|
A:HIS248
|
5.0
|
31.9
|
1.0
|
|
OD1
|
A:ASN124
|
5.0
|
27.1
|
1.0
|
|
HD1
|
A:HIS66
|
5.0
|
36.4
|
1.0
|
|
HZ
|
A:PHE267
|
5.0
|
38.9
|
1.0
|
|
Manganese binding site 9 out
of 12 in 6zee
Go back to
Manganese Binding Sites List in 6zee
Manganese binding site 9 out
of 12 in the Structure of PP1(7-300) Bound to PHACTR1 (507-580) at PH8.4
 Mono view
 Stereo pair view
|
|
A full contact list of Manganese with other atoms in the Mn binding
site number 9 of Structure of PP1(7-300) Bound to PHACTR1 (507-580) at PH8.4 within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
I:Mn501
b:34.5
occ:1.00
|
O4
|
I:SO4505
|
2.1
|
37.2
|
1.0
|
|
OD1
|
I:ASN124
|
2.1
|
39.7
|
1.0
|
|
ND1
|
I:HIS248
|
2.2
|
36.5
|
1.0
|
|
OD1
|
I:ASP92
|
2.2
|
40.5
|
1.0
|
|
NE2
|
I:HIS173
|
2.3
|
40.0
|
1.0
|
|
O
|
I:HOH603
|
2.6
|
38.2
|
1.0
|
|
HE1
|
I:HIS248
|
2.7
|
43.2
|
1.0
|
|
CE1
|
I:HIS248
|
2.8
|
35.9
|
1.0
|
|
HA
|
I:HIS248
|
2.9
|
45.0
|
1.0
|
|
CG
|
I:ASP92
|
3.1
|
40.8
|
1.0
|
|
CG
|
I:ASN124
|
3.1
|
39.0
|
1.0
|
|
HD21
|
I:ASN124
|
3.1
|
46.1
|
1.0
|
|
CE1
|
I:HIS173
|
3.2
|
40.4
|
1.0
|
|
MN
|
I:MN502
|
3.2
|
45.2
|
1.0
|
|
S
|
I:SO4505
|
3.3
|
42.0
|
1.0
|
|
CD2
|
I:HIS173
|
3.3
|
40.2
|
1.0
|
|
HE1
|
I:HIS173
|
3.4
|
47.7
|
1.0
|
|
OD2
|
I:ASP92
|
3.4
|
40.6
|
1.0
|
|
HD2
|
I:HIS173
|
3.5
|
47.4
|
1.0
|
|
CG
|
I:HIS248
|
3.5
|
36.6
|
1.0
|
|
ND2
|
I:ASN124
|
3.5
|
38.7
|
1.0
|
|
HD2
|
I:HIS125
|
3.5
|
50.5
|
1.0
|
|
O3
|
I:SO4505
|
3.7
|
39.5
|
1.0
|
|
O2
|
I:SO4505
|
3.7
|
35.0
|
1.0
|
|
CA
|
I:HIS248
|
3.8
|
37.4
|
1.0
|
|
H
|
I:ASN124
|
3.9
|
47.0
|
1.0
|
|
OD2
|
I:ASP64
|
3.9
|
39.6
|
1.0
|
|
O
|
I:HIS248
|
3.9
|
36.8
|
1.0
|
|
NE2
|
I:HIS248
|
4.1
|
35.6
|
1.0
|
|
CB
|
I:HIS248
|
4.1
|
38.2
|
1.0
|
|
HB2
|
I:HIS248
|
4.3
|
46.0
|
1.0
|
|
HD22
|
I:ASN124
|
4.3
|
46.1
|
1.0
|
|
C
|
I:HIS248
|
4.4
|
37.5
|
1.0
|
|
ND1
|
I:HIS173
|
4.4
|
40.9
|
1.0
|
|
CD2
|
I:HIS125
|
4.4
|
41.9
|
1.0
|
|
CD2
|
I:HIS248
|
4.4
|
36.9
|
1.0
|
|
CB
|
I:ASP92
|
4.4
|
41.5
|
1.0
|
|
CG
|
I:HIS173
|
4.4
|
40.8
|
1.0
|
|
O1
|
I:SO4505
|
4.5
|
33.4
|
1.0
|
|
CB
|
I:ASN124
|
4.5
|
38.9
|
1.0
|
|
HB2
|
I:ASP92
|
4.5
|
49.0
|
1.0
|
|
HB3
|
I:ASN124
|
4.6
|
45.8
|
1.0
|
|
HH12
|
I:ARG221
|
4.6
|
46.1
|
1.0
|
|
N
|
I:ASN124
|
4.6
|
39.8
|
1.0
|
|
HB3
|
I:ASP92
|
4.7
|
49.0
|
1.0
|
|
O
|
I:LEU205
|
4.7
|
35.2
|
1.0
|
|
H
|
I:HIS125
|
4.7
|
48.4
|
1.0
|
|
HE2
|
I:HIS248
|
4.8
|
42.9
|
1.0
|
|
H
|
I:HIS248
|
4.8
|
44.7
|
1.0
|
|
CG
|
I:ASP64
|
4.8
|
40.5
|
1.0
|
|
N
|
I:HIS248
|
4.9
|
37.1
|
1.0
|
|
NE2
|
I:HIS66
|
4.9
|
44.1
|
1.0
|
|
HE2
|
I:HIS125
|
4.9
|
47.4
|
1.0
|
|
HB3
|
I:HIS248
|
5.0
|
46.0
|
1.0
|
|
Manganese binding site 10 out
of 12 in 6zee
Go back to
Manganese Binding Sites List in 6zee
Manganese binding site 10 out
of 12 in the Structure of PP1(7-300) Bound to PHACTR1 (507-580) at PH8.4
 Mono view
 Stereo pair view
|
|
A full contact list of Manganese with other atoms in the Mn binding
site number 10 of Structure of PP1(7-300) Bound to PHACTR1 (507-580) at PH8.4 within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
I:Mn502
b:45.2
occ:1.00
|
NE2
|
I:HIS66
|
1.9
|
44.1
|
1.0
|
|
O
|
I:HOH603
|
2.0
|
38.2
|
1.0
|
|
O3
|
I:SO4505
|
2.1
|
39.5
|
1.0
|
|
OD1
|
I:ASP92
|
2.1
|
40.5
|
1.0
|
|
OD2
|
I:ASP64
|
2.3
|
39.6
|
1.0
|
|
CE1
|
I:HIS66
|
2.9
|
43.5
|
1.0
|
|
CD2
|
I:HIS66
|
3.0
|
42.4
|
1.0
|
|
S
|
I:SO4505
|
3.1
|
42.0
|
1.0
|
|
HE1
|
I:HIS66
|
3.1
|
52.4
|
1.0
|
|
HD2
|
I:HIS66
|
3.2
|
51.0
|
1.0
|
|
CG
|
I:ASP92
|
3.2
|
40.8
|
1.0
|
|
HB3
|
I:ASP92
|
3.2
|
49.0
|
1.0
|
|
O4
|
I:SO4505
|
3.2
|
37.2
|
1.0
|
|
MN
|
I:MN501
|
3.2
|
34.5
|
1.0
|
|
HH12
|
I:ARG96
|
3.4
|
52.1
|
0.5
|
|
CG
|
I:ASP64
|
3.5
|
40.5
|
1.0
|
|
O2
|
I:SO4505
|
3.6
|
35.0
|
1.0
|
|
CB
|
I:ASP92
|
3.6
|
41.5
|
1.0
|
|
HD2
|
I:HIS125
|
3.8
|
50.5
|
1.0
|
|
HB3
|
I:ASP64
|
3.9
|
48.6
|
1.0
|
|
HB2
|
I:ASP92
|
3.9
|
49.0
|
1.0
|
|
HH11
|
I:ARG96
|
3.9
|
52.1
|
0.5
|
|
HE1
|
I:PHE267
|
3.9
|
46.5
|
1.0
|
|
NH1
|
I:ARG96
|
4.0
|
43.3
|
0.5
|
|
ND1
|
I:HIS66
|
4.0
|
43.5
|
1.0
|
|
CG
|
I:HIS66
|
4.1
|
43.8
|
1.0
|
|
OH
|
I:TYR272
|
4.1
|
45.1
|
1.0
|
|
HA
|
I:HIS248
|
4.2
|
45.0
|
1.0
|
|
HE1
|
I:HIS173
|
4.2
|
47.7
|
1.0
|
|
CD2
|
I:HIS125
|
4.2
|
41.9
|
1.0
|
|
CB
|
I:ASP64
|
4.3
|
41.2
|
1.0
|
|
OD2
|
I:ASP92
|
4.3
|
40.6
|
1.0
|
|
HH
|
I:TYR272
|
4.3
|
54.3
|
1.0
|
|
O1
|
I:SO4505
|
4.3
|
33.4
|
1.0
|
|
O
|
I:HIS248
|
4.3
|
36.8
|
1.0
|
|
HE2
|
I:HIS125
|
4.4
|
47.4
|
1.0
|
|
HE
|
I:ARG96
|
4.4
|
53.3
|
0.5
|
|
OD1
|
I:ASP64
|
4.4
|
40.9
|
1.0
|
|
NE2
|
I:HIS125
|
4.6
|
39.4
|
1.0
|
|
NE2
|
I:HIS173
|
4.7
|
40.0
|
1.0
|
|
HB2
|
I:ASP64
|
4.7
|
48.6
|
1.0
|
|
CE1
|
I:PHE267
|
4.7
|
38.6
|
1.0
|
|
CE1
|
I:HIS173
|
4.7
|
40.4
|
1.0
|
|
HD1
|
I:HIS66
|
4.8
|
52.3
|
1.0
|
|
OD1
|
I:ASN124
|
4.8
|
39.7
|
1.0
|
|
HZ
|
I:PHE267
|
4.8
|
46.9
|
1.0
|
|
ND1
|
I:HIS248
|
4.9
|
36.5
|
1.0
|
|
C
|
I:HIS248
|
4.9
|
37.5
|
1.0
|
|
CZ
|
I:TYR272
|
5.0
|
42.8
|
1.0
|
|
CA
|
I:HIS248
|
5.0
|
37.4
|
1.0
|
|
Reference:
R.O.Fedoryshchak,
M.Prechova,
A.Butler,
R.Lee,
N.O'reilly,
H.R.Flynn,
A.P.Snijders,
N.Eder,
S.Ultanir,
S.Mouilleron,
R.Treisman.
Molecular Basis For Substrate Specificity of the PHACTR1/PP1 Phosphatase Holoenzyme. Elife V. 9 2020.
ISSN: ESSN 2050-084X
PubMed: 32975518
DOI: 10.7554/ELIFE.61509
Page generated: Tue Dec 15 05:09:46 2020
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