Manganese in PDB 5zt0: Crystal Structure of Protein Phosphate 1 Complexed with PP1 Binding Domain of Gl
Enzymatic activity of Crystal Structure of Protein Phosphate 1 Complexed with PP1 Binding Domain of Gl
All present enzymatic activity of Crystal Structure of Protein Phosphate 1 Complexed with PP1 Binding Domain of Gl:
3.1.3.16;
Protein crystallography data
The structure of Crystal Structure of Protein Phosphate 1 Complexed with PP1 Binding Domain of Gl, PDB code: 5zt0
was solved by
J.Yu,
S.Xiang,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
|
Resolution Low / High (Å)
|
41.79 /
3.32
|
|
Space group
|
P 32
|
|
Cell size a, b, c (Å), α, β, γ (°)
|
106.530,
106.530,
187.510,
90.00,
90.00,
120.00
|
|
R / Rfree (%)
|
20 /
23.3
|
Manganese Binding Sites:
Pages:
>>> Page 1 <<<
Page 2, Binding sites: 11 -
12;
Binding sites:
The binding sites of Manganese atom in the Crystal Structure of Protein Phosphate 1 Complexed with PP1 Binding Domain of Gl
(pdb code 5zt0). This binding sites where shown within
5.0 Angstroms radius around Manganese atom.
In total 12 binding sites of Manganese where determined in the
Crystal Structure of Protein Phosphate 1 Complexed with PP1 Binding Domain of Gl, PDB code: 5zt0:
Jump to Manganese binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
9;
10;
Manganese binding site 1 out
of 12 in 5zt0
Go back to
Manganese Binding Sites List in 5zt0
Manganese binding site 1 out
of 12 in the Crystal Structure of Protein Phosphate 1 Complexed with PP1 Binding Domain of Gl
 Mono view
 Stereo pair view
|
|
A full contact list of Manganese with other atoms in the Mn binding
site number 1 of Crystal Structure of Protein Phosphate 1 Complexed with PP1 Binding Domain of Gl within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mn401
b:47.4
occ:1.00
|
OD2
|
A:ASP92
|
1.9
|
0.6
|
1.0
|
|
MN
|
A:MN402
|
2.0
|
31.8
|
0.5
|
|
NE2
|
A:HIS173
|
2.5
|
90.1
|
1.0
|
|
ND1
|
A:HIS248
|
2.5
|
91.6
|
1.0
|
|
OD1
|
A:ASN124
|
2.5
|
76.1
|
1.0
|
|
O3
|
A:PO4403
|
2.7
|
29.6
|
0.8
|
|
CG
|
A:ASP92
|
2.8
|
71.8
|
1.0
|
|
CE1
|
A:HIS173
|
3.1
|
85.1
|
1.0
|
|
OD1
|
A:ASP92
|
3.1
|
71.7
|
1.0
|
|
CE1
|
A:HIS248
|
3.2
|
82.7
|
1.0
|
|
CG
|
A:ASN124
|
3.3
|
76.6
|
1.0
|
|
ND2
|
A:ASN124
|
3.5
|
76.8
|
1.0
|
|
CA
|
A:HIS248
|
3.5
|
74.5
|
1.0
|
|
CG
|
A:HIS248
|
3.6
|
88.2
|
1.0
|
|
CD2
|
A:HIS173
|
3.6
|
97.3
|
1.0
|
|
OD2
|
A:ASP64
|
3.6
|
74.0
|
1.0
|
|
O
|
A:HIS248
|
3.8
|
74.6
|
1.0
|
|
P
|
A:PO4403
|
3.8
|
52.0
|
0.8
|
|
CD2
|
A:HIS125
|
4.0
|
74.8
|
1.0
|
|
O4
|
A:PO4403
|
4.0
|
58.4
|
0.8
|
|
CB
|
A:HIS248
|
4.0
|
75.5
|
1.0
|
|
C
|
A:HIS248
|
4.1
|
75.0
|
1.0
|
|
CB
|
A:ASP92
|
4.2
|
0.8
|
1.0
|
|
NE2
|
A:HIS66
|
4.3
|
72.1
|
1.0
|
|
NE2
|
A:HIS125
|
4.4
|
75.0
|
1.0
|
|
ND1
|
A:HIS173
|
4.4
|
91.3
|
1.0
|
|
CG
|
A:ASP64
|
4.4
|
73.3
|
1.0
|
|
NE2
|
A:HIS248
|
4.4
|
89.1
|
1.0
|
|
O2
|
A:PO4403
|
4.4
|
66.7
|
0.8
|
|
OD1
|
A:ASP64
|
4.4
|
95.8
|
1.0
|
|
N
|
A:HIS248
|
4.6
|
74.9
|
1.0
|
|
CD2
|
A:HIS248
|
4.6
|
76.2
|
1.0
|
|
CG
|
A:HIS173
|
4.6
|
96.1
|
1.0
|
|
CB
|
A:ASN124
|
4.8
|
77.3
|
1.0
|
|
CE1
|
A:HIS66
|
4.8
|
71.2
|
1.0
|
|
N
|
A:ASN124
|
4.9
|
76.4
|
1.0
|
|
Manganese binding site 2 out
of 12 in 5zt0
Go back to
Manganese Binding Sites List in 5zt0
Manganese binding site 2 out
of 12 in the Crystal Structure of Protein Phosphate 1 Complexed with PP1 Binding Domain of Gl
 Mono view
 Stereo pair view
|
|
A full contact list of Manganese with other atoms in the Mn binding
site number 2 of Crystal Structure of Protein Phosphate 1 Complexed with PP1 Binding Domain of Gl within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mn402
b:31.8
occ:0.50
|
OD2
|
A:ASP92
|
1.8
|
0.6
|
1.0
|
|
MN
|
A:MN401
|
2.0
|
47.4
|
1.0
|
|
O4
|
A:PO4403
|
2.3
|
58.4
|
0.8
|
|
O3
|
A:PO4403
|
2.5
|
29.6
|
0.8
|
|
NE2
|
A:HIS66
|
2.6
|
72.1
|
1.0
|
|
P
|
A:PO4403
|
2.9
|
52.0
|
0.8
|
|
OD2
|
A:ASP64
|
2.9
|
74.0
|
1.0
|
|
CG
|
A:ASP92
|
3.0
|
71.8
|
1.0
|
|
CE1
|
A:HIS66
|
3.4
|
71.2
|
1.0
|
|
NE2
|
A:HIS125
|
3.6
|
75.0
|
1.0
|
|
O2
|
A:PO4403
|
3.7
|
66.7
|
0.8
|
|
CD2
|
A:HIS125
|
3.7
|
74.8
|
1.0
|
|
CD2
|
A:HIS66
|
3.7
|
71.9
|
1.0
|
|
OD1
|
A:ASP92
|
3.7
|
71.7
|
1.0
|
|
CG
|
A:ASP64
|
3.9
|
73.3
|
1.0
|
|
CB
|
A:ASP92
|
3.9
|
0.8
|
1.0
|
|
ND1
|
A:HIS248
|
4.0
|
91.6
|
1.0
|
|
O
|
A:HIS248
|
4.1
|
74.6
|
1.0
|
|
OD1
|
A:ASN124
|
4.1
|
76.1
|
1.0
|
|
O1
|
A:PO4403
|
4.2
|
34.5
|
0.8
|
|
NE2
|
A:HIS173
|
4.3
|
90.1
|
1.0
|
|
CA
|
A:HIS248
|
4.4
|
74.5
|
1.0
|
|
C
|
A:HIS248
|
4.5
|
75.0
|
1.0
|
|
OD1
|
A:ASP64
|
4.5
|
95.8
|
1.0
|
|
CE1
|
A:HIS173
|
4.5
|
85.1
|
1.0
|
|
ND1
|
A:HIS66
|
4.6
|
70.5
|
1.0
|
|
OH
|
A:TYR272
|
4.6
|
0.5
|
1.0
|
|
ND2
|
A:ASN124
|
4.6
|
76.8
|
1.0
|
|
CE1
|
A:HIS248
|
4.6
|
82.7
|
1.0
|
|
CE1
|
A:HIS125
|
4.8
|
74.9
|
1.0
|
|
CG
|
A:HIS66
|
4.8
|
70.8
|
1.0
|
|
CG
|
A:ASN124
|
4.8
|
76.6
|
1.0
|
|
CB
|
A:ASP64
|
4.9
|
72.7
|
1.0
|
|
CG
|
A:HIS125
|
4.9
|
74.5
|
1.0
|
|
Manganese binding site 3 out
of 12 in 5zt0
Go back to
Manganese Binding Sites List in 5zt0
Manganese binding site 3 out
of 12 in the Crystal Structure of Protein Phosphate 1 Complexed with PP1 Binding Domain of Gl
 Mono view
 Stereo pair view
|
|
A full contact list of Manganese with other atoms in the Mn binding
site number 3 of Crystal Structure of Protein Phosphate 1 Complexed with PP1 Binding Domain of Gl within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mn401
b:0.6
occ:1.00
|
OD1
|
B:ASN124
|
2.1
|
80.4
|
1.0
|
|
OD2
|
B:ASP92
|
2.2
|
84.8
|
1.0
|
|
O3
|
B:PO4403
|
2.3
|
18.6
|
0.8
|
|
ND1
|
B:HIS248
|
2.7
|
0.2
|
1.0
|
|
MN
|
B:MN402
|
2.8
|
54.6
|
0.5
|
|
CG
|
B:ASN124
|
2.8
|
81.1
|
1.0
|
|
ND2
|
B:ASN124
|
2.9
|
81.8
|
1.0
|
|
CG
|
B:ASP92
|
2.9
|
82.8
|
1.0
|
|
NE2
|
B:HIS173
|
2.9
|
0.6
|
1.0
|
|
OD1
|
B:ASP92
|
3.0
|
82.6
|
1.0
|
|
CE1
|
B:HIS248
|
3.1
|
0.4
|
1.0
|
|
P
|
B:PO4403
|
3.2
|
68.4
|
0.8
|
|
CD2
|
B:HIS125
|
3.3
|
0.4
|
1.0
|
|
O2
|
B:PO4403
|
3.4
|
71.6
|
0.8
|
|
O4
|
B:PO4403
|
3.6
|
83.5
|
0.8
|
|
CE1
|
B:HIS173
|
3.7
|
0.6
|
1.0
|
|
NE2
|
B:HIS125
|
3.8
|
81.2
|
1.0
|
|
CG
|
B:HIS248
|
4.0
|
0.8
|
1.0
|
|
CD2
|
B:HIS173
|
4.0
|
97.5
|
1.0
|
|
O
|
B:HIS248
|
4.3
|
91.3
|
1.0
|
|
CA
|
B:HIS248
|
4.3
|
97.0
|
1.0
|
|
CB
|
B:ASN124
|
4.3
|
81.1
|
1.0
|
|
NE2
|
B:HIS248
|
4.4
|
0.6
|
1.0
|
|
CB
|
B:ASP92
|
4.4
|
85.5
|
1.0
|
|
OD2
|
B:ASP64
|
4.5
|
97.2
|
1.0
|
|
NE2
|
B:HIS66
|
4.6
|
70.9
|
1.0
|
|
CG
|
B:HIS125
|
4.6
|
79.8
|
1.0
|
|
O1
|
B:PO4403
|
4.6
|
61.2
|
0.8
|
|
CB
|
B:HIS248
|
4.6
|
0.8
|
1.0
|
|
N
|
B:ASN124
|
4.7
|
79.3
|
1.0
|
|
C
|
B:HIS248
|
4.8
|
96.2
|
1.0
|
|
CD2
|
B:HIS248
|
4.8
|
0.6
|
1.0
|
|
N
|
B:HIS125
|
4.9
|
79.2
|
1.0
|
|
O
|
B:LEU205
|
4.9
|
92.9
|
1.0
|
|
ND1
|
B:HIS173
|
4.9
|
0.6
|
1.0
|
|
CE1
|
B:HIS66
|
5.0
|
70.5
|
1.0
|
|
Manganese binding site 4 out
of 12 in 5zt0
Go back to
Manganese Binding Sites List in 5zt0
Manganese binding site 4 out
of 12 in the Crystal Structure of Protein Phosphate 1 Complexed with PP1 Binding Domain of Gl
 Mono view
 Stereo pair view
|
|
A full contact list of Manganese with other atoms in the Mn binding
site number 4 of Crystal Structure of Protein Phosphate 1 Complexed with PP1 Binding Domain of Gl within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mn402
b:54.6
occ:0.50
|
OD2
|
B:ASP92
|
2.1
|
84.8
|
1.0
|
|
O2
|
B:PO4403
|
2.2
|
71.6
|
0.8
|
|
OD2
|
B:ASP64
|
2.6
|
97.2
|
1.0
|
|
NE2
|
B:HIS66
|
2.7
|
70.9
|
1.0
|
|
MN
|
B:MN401
|
2.8
|
0.6
|
1.0
|
|
P
|
B:PO4403
|
3.3
|
68.4
|
0.8
|
|
CG
|
B:ASP92
|
3.3
|
82.8
|
1.0
|
|
CD2
|
B:HIS66
|
3.4
|
70.5
|
1.0
|
|
O3
|
B:PO4403
|
3.6
|
18.6
|
0.8
|
|
CG
|
B:ASP64
|
3.6
|
91.9
|
1.0
|
|
O4
|
B:PO4403
|
3.7
|
83.5
|
0.8
|
|
CE1
|
B:HIS66
|
3.8
|
70.5
|
1.0
|
|
O
|
B:HIS248
|
3.9
|
91.3
|
1.0
|
|
CB
|
B:ASP92
|
4.1
|
85.5
|
1.0
|
|
OH
|
B:TYR272
|
4.1
|
0.1
|
1.0
|
|
OD1
|
B:ASP92
|
4.2
|
82.6
|
1.0
|
|
NE2
|
B:HIS125
|
4.3
|
81.2
|
1.0
|
|
OD1
|
B:ASP64
|
4.3
|
95.2
|
1.0
|
|
CD2
|
B:HIS125
|
4.3
|
0.4
|
1.0
|
|
C
|
B:HIS248
|
4.3
|
96.2
|
1.0
|
|
ND1
|
B:HIS248
|
4.4
|
0.2
|
1.0
|
|
CA
|
B:HIS248
|
4.4
|
97.0
|
1.0
|
|
CB
|
B:ASP64
|
4.6
|
74.4
|
1.0
|
|
O1
|
B:PO4403
|
4.6
|
61.2
|
0.8
|
|
CE1
|
B:PHE267
|
4.7
|
0.7
|
1.0
|
|
CG
|
B:HIS66
|
4.7
|
69.8
|
1.0
|
|
NE2
|
B:HIS173
|
4.7
|
0.6
|
1.0
|
|
CE1
|
B:HIS173
|
4.8
|
0.6
|
1.0
|
|
ND1
|
B:HIS66
|
4.8
|
69.8
|
1.0
|
|
OD1
|
B:ASN124
|
4.8
|
80.4
|
1.0
|
|
CZ
|
B:TYR272
|
4.9
|
0.8
|
1.0
|
|
Manganese binding site 5 out
of 12 in 5zt0
Go back to
Manganese Binding Sites List in 5zt0
Manganese binding site 5 out
of 12 in the Crystal Structure of Protein Phosphate 1 Complexed with PP1 Binding Domain of Gl
 Mono view
 Stereo pair view
|
|
A full contact list of Manganese with other atoms in the Mn binding
site number 5 of Crystal Structure of Protein Phosphate 1 Complexed with PP1 Binding Domain of Gl within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Mn401
b:65.7
occ:1.00
|
OD1
|
C:ASN124
|
2.0
|
0.2
|
1.0
|
|
O3
|
C:PO4403
|
2.1
|
18.4
|
0.8
|
|
OD2
|
C:ASP92
|
2.4
|
74.1
|
1.0
|
|
ND1
|
C:HIS248
|
2.4
|
99.8
|
1.0
|
|
NE2
|
C:HIS173
|
2.7
|
68.5
|
1.0
|
|
CG
|
C:ASN124
|
2.7
|
71.0
|
1.0
|
|
ND2
|
C:ASN124
|
2.9
|
71.5
|
1.0
|
|
CE1
|
C:HIS248
|
2.9
|
96.1
|
1.0
|
|
MN
|
C:MN402
|
2.9
|
21.6
|
0.5
|
|
CG
|
C:ASP92
|
3.1
|
74.0
|
1.0
|
|
OD1
|
C:ASP92
|
3.1
|
74.4
|
1.0
|
|
P
|
C:PO4403
|
3.2
|
65.0
|
0.8
|
|
O1
|
C:PO4403
|
3.3
|
67.5
|
0.8
|
|
CE1
|
C:HIS173
|
3.5
|
68.9
|
1.0
|
|
CG
|
C:HIS248
|
3.6
|
76.3
|
1.0
|
|
CD2
|
C:HIS125
|
3.7
|
81.1
|
1.0
|
|
CD2
|
C:HIS173
|
3.8
|
69.7
|
1.0
|
|
O
|
C:HIS248
|
4.0
|
97.2
|
1.0
|
|
O4
|
C:PO4403
|
4.0
|
77.3
|
0.8
|
|
CA
|
C:HIS248
|
4.0
|
75.3
|
1.0
|
|
OD2
|
C:ASP64
|
4.1
|
73.5
|
1.0
|
|
NE2
|
C:HIS248
|
4.1
|
86.6
|
1.0
|
|
NE2
|
C:HIS125
|
4.1
|
70.9
|
1.0
|
|
CB
|
C:ASN124
|
4.2
|
71.1
|
1.0
|
|
CB
|
C:HIS248
|
4.3
|
76.4
|
1.0
|
|
O2
|
C:PO4403
|
4.4
|
0.5
|
0.8
|
|
C
|
C:HIS248
|
4.5
|
75.6
|
1.0
|
|
CB
|
C:ASP92
|
4.5
|
96.6
|
1.0
|
|
CD2
|
C:HIS248
|
4.5
|
88.0
|
1.0
|
|
N
|
C:ASN124
|
4.6
|
70.0
|
1.0
|
|
ND1
|
C:HIS173
|
4.7
|
70.4
|
1.0
|
|
NE2
|
C:HIS66
|
4.8
|
85.4
|
1.0
|
|
O
|
C:LEU205
|
4.8
|
71.7
|
1.0
|
|
CA
|
C:ASN124
|
4.9
|
70.5
|
1.0
|
|
CG
|
C:HIS173
|
4.9
|
71.2
|
1.0
|
|
CG
|
C:HIS125
|
4.9
|
72.2
|
1.0
|
|
CG
|
C:ASP64
|
4.9
|
73.2
|
1.0
|
|
Manganese binding site 6 out
of 12 in 5zt0
Go back to
Manganese Binding Sites List in 5zt0
Manganese binding site 6 out
of 12 in the Crystal Structure of Protein Phosphate 1 Complexed with PP1 Binding Domain of Gl
 Mono view
 Stereo pair view
|
|
A full contact list of Manganese with other atoms in the Mn binding
site number 6 of Crystal Structure of Protein Phosphate 1 Complexed with PP1 Binding Domain of Gl within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Mn402
b:21.6
occ:0.50
|
OD2
|
C:ASP92
|
1.9
|
74.1
|
1.0
|
|
OD2
|
C:ASP64
|
1.9
|
73.5
|
1.0
|
|
O1
|
C:PO4403
|
2.1
|
67.5
|
0.8
|
|
NE2
|
C:HIS66
|
2.7
|
85.4
|
1.0
|
|
MN
|
C:MN401
|
2.9
|
65.7
|
1.0
|
|
CG
|
C:ASP64
|
3.0
|
73.2
|
1.0
|
|
CG
|
C:ASP92
|
3.0
|
74.0
|
1.0
|
|
P
|
C:PO4403
|
3.2
|
65.0
|
0.8
|
|
O3
|
C:PO4403
|
3.5
|
18.4
|
0.8
|
|
CD2
|
C:HIS66
|
3.5
|
73.7
|
1.0
|
|
O
|
C:HIS248
|
3.6
|
97.2
|
1.0
|
|
CB
|
C:ASP92
|
3.7
|
96.6
|
1.0
|
|
CE1
|
C:HIS66
|
3.7
|
74.1
|
1.0
|
|
OD1
|
C:ASP64
|
3.8
|
74.8
|
1.0
|
|
O4
|
C:PO4403
|
3.9
|
77.3
|
0.8
|
|
CB
|
C:ASP64
|
3.9
|
88.0
|
1.0
|
|
C
|
C:HIS248
|
4.0
|
75.6
|
1.0
|
|
CA
|
C:HIS248
|
4.0
|
75.3
|
1.0
|
|
OD1
|
C:ASP92
|
4.0
|
74.4
|
1.0
|
|
ND1
|
C:HIS248
|
4.3
|
99.8
|
1.0
|
|
CE1
|
C:HIS173
|
4.3
|
68.9
|
1.0
|
|
CE1
|
C:PHE267
|
4.4
|
82.7
|
1.0
|
|
NE2
|
C:HIS173
|
4.4
|
68.5
|
1.0
|
|
O2
|
C:PO4403
|
4.4
|
0.5
|
0.8
|
|
CD2
|
C:HIS125
|
4.5
|
81.1
|
1.0
|
|
NE2
|
C:HIS125
|
4.6
|
70.9
|
1.0
|
|
OH
|
C:TYR272
|
4.6
|
84.3
|
1.0
|
|
CG
|
C:HIS66
|
4.7
|
73.6
|
1.0
|
|
N
|
C:HIS248
|
4.7
|
79.2
|
1.0
|
|
OD1
|
C:ASN124
|
4.7
|
0.2
|
1.0
|
|
ND1
|
C:HIS66
|
4.8
|
73.9
|
1.0
|
|
CZ
|
C:PHE267
|
4.8
|
83.3
|
1.0
|
|
N
|
C:GLN249
|
4.9
|
76.5
|
1.0
|
|
Manganese binding site 7 out
of 12 in 5zt0
Go back to
Manganese Binding Sites List in 5zt0
Manganese binding site 7 out
of 12 in the Crystal Structure of Protein Phosphate 1 Complexed with PP1 Binding Domain of Gl
 Mono view
 Stereo pair view
|
|
A full contact list of Manganese with other atoms in the Mn binding
site number 7 of Crystal Structure of Protein Phosphate 1 Complexed with PP1 Binding Domain of Gl within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Mn401
b:47.3
occ:1.00
|
OD2
|
D:ASP92
|
2.0
|
77.3
|
1.0
|
|
O1
|
D:PO4403
|
2.3
|
25.9
|
0.8
|
|
OD1
|
D:ASN124
|
2.4
|
78.0
|
1.0
|
|
ND1
|
D:HIS248
|
2.5
|
91.4
|
1.0
|
|
NE2
|
D:HIS173
|
2.6
|
0.6
|
1.0
|
|
MN
|
D:MN402
|
2.7
|
56.4
|
0.5
|
|
CG
|
D:ASP92
|
2.8
|
75.9
|
1.0
|
|
OD1
|
D:ASP92
|
3.0
|
75.2
|
1.0
|
|
CG
|
D:ASN124
|
3.3
|
78.7
|
1.0
|
|
CE1
|
D:HIS173
|
3.3
|
0.1
|
1.0
|
|
CE1
|
D:HIS248
|
3.3
|
85.6
|
1.0
|
|
P
|
D:PO4403
|
3.4
|
65.1
|
0.8
|
|
O3
|
D:PO4403
|
3.4
|
49.1
|
0.8
|
|
ND2
|
D:ASN124
|
3.4
|
79.2
|
1.0
|
|
CA
|
D:HIS248
|
3.6
|
81.3
|
1.0
|
|
CG
|
D:HIS248
|
3.6
|
82.2
|
1.0
|
|
O
|
D:HIS248
|
3.8
|
82.5
|
1.0
|
|
CD2
|
D:HIS173
|
3.8
|
0.7
|
1.0
|
|
OD2
|
D:ASP64
|
3.8
|
83.4
|
1.0
|
|
CD2
|
D:HIS125
|
3.8
|
84.8
|
1.0
|
|
CB
|
D:HIS248
|
4.0
|
82.2
|
1.0
|
|
NE2
|
D:HIS125
|
4.1
|
78.0
|
1.0
|
|
C
|
D:HIS248
|
4.1
|
85.0
|
1.0
|
|
O2
|
D:PO4403
|
4.2
|
0.5
|
0.8
|
|
CB
|
D:ASP92
|
4.3
|
83.5
|
1.0
|
|
NE2
|
D:HIS248
|
4.5
|
83.2
|
1.0
|
|
NE2
|
D:HIS66
|
4.5
|
88.6
|
1.0
|
|
CG
|
D:ASP64
|
4.5
|
93.3
|
1.0
|
|
ND1
|
D:HIS173
|
4.5
|
0.7
|
1.0
|
|
O4
|
D:PO4403
|
4.6
|
65.3
|
0.8
|
|
N
|
D:HIS248
|
4.6
|
81.3
|
1.0
|
|
OD1
|
D:ASP64
|
4.6
|
0.2
|
1.0
|
|
CD2
|
D:HIS248
|
4.7
|
85.2
|
1.0
|
|
CB
|
D:ASN124
|
4.7
|
79.2
|
1.0
|
|
CG
|
D:HIS173
|
4.8
|
0.0
|
1.0
|
|
N
|
D:ASN124
|
5.0
|
0.0
|
1.0
|
|
Manganese binding site 8 out
of 12 in 5zt0
Go back to
Manganese Binding Sites List in 5zt0
Manganese binding site 8 out
of 12 in the Crystal Structure of Protein Phosphate 1 Complexed with PP1 Binding Domain of Gl
 Mono view
 Stereo pair view
|
|
A full contact list of Manganese with other atoms in the Mn binding
site number 8 of Crystal Structure of Protein Phosphate 1 Complexed with PP1 Binding Domain of Gl within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Mn402
b:56.4
occ:0.50
|
O3
|
D:PO4403
|
2.0
|
49.1
|
0.8
|
|
OD2
|
D:ASP64
|
2.2
|
83.4
|
1.0
|
|
OD2
|
D:ASP92
|
2.2
|
77.3
|
1.0
|
|
MN
|
D:MN401
|
2.7
|
47.3
|
1.0
|
|
NE2
|
D:HIS66
|
2.8
|
88.6
|
1.0
|
|
P
|
D:PO4403
|
3.2
|
65.1
|
0.8
|
|
CG
|
D:ASP64
|
3.3
|
93.3
|
1.0
|
|
O1
|
D:PO4403
|
3.3
|
25.9
|
0.8
|
|
CG
|
D:ASP92
|
3.4
|
75.9
|
1.0
|
|
CD2
|
D:HIS66
|
3.5
|
93.3
|
1.0
|
|
O
|
D:HIS248
|
3.8
|
82.5
|
1.0
|
|
CE1
|
D:HIS66
|
3.9
|
85.7
|
1.0
|
|
C
|
D:HIS248
|
4.0
|
85.0
|
1.0
|
|
OD1
|
D:ASP64
|
4.1
|
0.2
|
1.0
|
|
CB
|
D:ASP92
|
4.1
|
83.5
|
1.0
|
|
CE1
|
D:PHE267
|
4.1
|
0.9
|
1.0
|
|
CB
|
D:ASP64
|
4.1
|
94.0
|
1.0
|
|
CA
|
D:HIS248
|
4.1
|
81.3
|
1.0
|
|
O2
|
D:PO4403
|
4.2
|
0.5
|
0.8
|
|
O4
|
D:PO4403
|
4.2
|
65.3
|
0.8
|
|
OH
|
D:TYR272
|
4.3
|
0.5
|
1.0
|
|
OD1
|
D:ASP92
|
4.4
|
75.2
|
1.0
|
|
NE2
|
D:HIS125
|
4.5
|
78.0
|
1.0
|
|
ND1
|
D:HIS248
|
4.5
|
91.4
|
1.0
|
|
CZ
|
D:PHE267
|
4.6
|
0.6
|
1.0
|
|
CD2
|
D:HIS125
|
4.7
|
84.8
|
1.0
|
|
CE1
|
D:HIS173
|
4.7
|
0.1
|
1.0
|
|
NE2
|
D:HIS173
|
4.7
|
0.6
|
1.0
|
|
CG
|
D:HIS66
|
4.7
|
0.7
|
1.0
|
|
N
|
D:HIS248
|
4.8
|
81.3
|
1.0
|
|
N
|
D:GLN249
|
4.8
|
88.0
|
1.0
|
|
ND1
|
D:HIS66
|
4.9
|
99.6
|
1.0
|
|
CZ
|
D:TYR272
|
4.9
|
0.4
|
1.0
|
|
Manganese binding site 9 out
of 12 in 5zt0
Go back to
Manganese Binding Sites List in 5zt0
Manganese binding site 9 out
of 12 in the Crystal Structure of Protein Phosphate 1 Complexed with PP1 Binding Domain of Gl
 Mono view
 Stereo pair view
|
|
A full contact list of Manganese with other atoms in the Mn binding
site number 9 of Crystal Structure of Protein Phosphate 1 Complexed with PP1 Binding Domain of Gl within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Mn401
b:68.9
occ:1.00
|
OD1
|
E:ASN124
|
1.9
|
0.0
|
1.0
|
|
O1
|
E:PO4403
|
2.2
|
21.4
|
0.8
|
|
ND1
|
E:HIS248
|
2.4
|
0.3
|
1.0
|
|
OD2
|
E:ASP92
|
2.5
|
0.3
|
1.0
|
|
CG
|
E:ASN124
|
2.6
|
96.4
|
1.0
|
|
ND2
|
E:ASN124
|
2.7
|
88.2
|
1.0
|
|
NE2
|
E:HIS173
|
2.8
|
0.2
|
1.0
|
|
MN
|
E:MN402
|
2.8
|
44.9
|
0.5
|
|
CE1
|
E:HIS248
|
2.8
|
0.3
|
1.0
|
|
OD1
|
E:ASP92
|
3.2
|
86.8
|
1.0
|
|
CG
|
E:ASP92
|
3.3
|
85.5
|
1.0
|
|
P
|
E:PO4403
|
3.4
|
66.0
|
0.8
|
|
CD2
|
E:HIS125
|
3.6
|
90.5
|
1.0
|
|
CE1
|
E:HIS173
|
3.6
|
0.7
|
1.0
|
|
O3
|
E:PO4403
|
3.7
|
71.3
|
0.8
|
|
CG
|
E:HIS248
|
3.7
|
0.1
|
1.0
|
|
CD2
|
E:HIS173
|
3.8
|
0.2
|
1.0
|
|
NE2
|
E:HIS125
|
4.0
|
87.6
|
1.0
|
|
NE2
|
E:HIS248
|
4.0
|
96.8
|
1.0
|
|
O
|
E:HIS248
|
4.1
|
0.2
|
1.0
|
|
CB
|
E:ASN124
|
4.1
|
95.3
|
1.0
|
|
O4
|
E:PO4403
|
4.1
|
0.1
|
0.8
|
|
CA
|
E:HIS248
|
4.1
|
0.3
|
1.0
|
|
CB
|
E:HIS248
|
4.4
|
0.3
|
1.0
|
|
CD2
|
E:HIS248
|
4.5
|
98.1
|
1.0
|
|
OD2
|
E:ASP64
|
4.5
|
0.7
|
1.0
|
|
N
|
E:ASN124
|
4.6
|
0.4
|
1.0
|
|
C
|
E:HIS248
|
4.6
|
0.6
|
1.0
|
|
O2
|
E:PO4403
|
4.6
|
70.4
|
0.8
|
|
O
|
E:LEU205
|
4.7
|
0.9
|
1.0
|
|
CB
|
E:ASP92
|
4.7
|
84.8
|
1.0
|
|
ND1
|
E:HIS173
|
4.8
|
0.3
|
1.0
|
|
CA
|
E:ASN124
|
4.9
|
0.2
|
1.0
|
|
CG
|
E:HIS173
|
4.9
|
0.3
|
1.0
|
|
CG
|
E:HIS125
|
4.9
|
92.6
|
1.0
|
|
NE2
|
E:HIS66
|
5.0
|
0.7
|
1.0
|
|
Manganese binding site 10 out
of 12 in 5zt0
Go back to
Manganese Binding Sites List in 5zt0
Manganese binding site 10 out
of 12 in the Crystal Structure of Protein Phosphate 1 Complexed with PP1 Binding Domain of Gl
 Mono view
 Stereo pair view
|
|
A full contact list of Manganese with other atoms in the Mn binding
site number 10 of Crystal Structure of Protein Phosphate 1 Complexed with PP1 Binding Domain of Gl within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Mn402
b:44.9
occ:0.50
|
OD2
|
E:ASP92
|
1.7
|
0.3
|
1.0
|
|
O3
|
E:PO4403
|
2.4
|
71.3
|
0.8
|
|
NE2
|
E:HIS66
|
2.5
|
0.7
|
1.0
|
|
OD2
|
E:ASP64
|
2.7
|
0.7
|
1.0
|
|
MN
|
E:MN401
|
2.8
|
68.9
|
1.0
|
|
CG
|
E:ASP92
|
2.9
|
85.5
|
1.0
|
|
O1
|
E:PO4403
|
3.2
|
21.4
|
0.8
|
|
CE1
|
E:HIS66
|
3.2
|
0.1
|
1.0
|
|
P
|
E:PO4403
|
3.3
|
66.0
|
0.8
|
|
CD2
|
E:HIS66
|
3.6
|
0.4
|
1.0
|
|
CG
|
E:ASP64
|
3.7
|
97.0
|
1.0
|
|
NE2
|
E:HIS125
|
3.7
|
87.6
|
1.0
|
|
OD1
|
E:ASP92
|
3.7
|
86.8
|
1.0
|
|
CB
|
E:ASP92
|
3.8
|
84.8
|
1.0
|
|
O
|
E:HIS248
|
3.8
|
0.2
|
1.0
|
|
CD2
|
E:HIS125
|
3.8
|
90.5
|
1.0
|
|
O4
|
E:PO4403
|
3.9
|
0.1
|
0.8
|
|
NH1
|
E:ARG96
|
4.0
|
82.7
|
1.0
|
|
OH
|
E:TYR272
|
4.1
|
0.7
|
1.0
|
|
ND1
|
E:HIS248
|
4.3
|
0.3
|
1.0
|
|
OD1
|
E:ASP64
|
4.3
|
89.3
|
1.0
|
|
OD1
|
E:ASN124
|
4.3
|
0.0
|
1.0
|
|
ND1
|
E:HIS66
|
4.4
|
1.0
|
1.0
|
|
NE2
|
E:HIS173
|
4.4
|
0.2
|
1.0
|
|
C
|
E:HIS248
|
4.5
|
0.6
|
1.0
|
|
CA
|
E:HIS248
|
4.5
|
0.3
|
1.0
|
|
CE1
|
E:HIS173
|
4.5
|
0.7
|
1.0
|
|
O2
|
E:PO4403
|
4.6
|
70.4
|
0.8
|
|
CB
|
E:ASP64
|
4.6
|
0.1
|
1.0
|
|
CG
|
E:HIS66
|
4.6
|
0.5
|
1.0
|
|
CE1
|
E:HIS125
|
4.8
|
94.3
|
1.0
|
|
CG
|
E:HIS125
|
4.9
|
92.6
|
1.0
|
|
ND2
|
E:ASN124
|
4.9
|
88.2
|
1.0
|
|
CE1
|
E:HIS248
|
5.0
|
0.3
|
1.0
|
|
CE1
|
E:PHE267
|
5.0
|
0.8
|
1.0
|
|
Reference:
J.Yu,
T.Deng,
S.Xiang.
Structural Basis For Protein Phosphatase 1 Recruitment By Glycogen-Targeting Subunits Febs J. V. 285 4646 2018.
ISSN: ISSN 1742-4658
PubMed: 30422398
DOI: 10.1111/FEBS.14699
Page generated: Sun Oct 6 03:45:22 2024
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