Manganese in PDB 4v0w: The Crystal Structure of Mouse PP1G in Complex with Truncated Human PPP1R15B (631-669)
Enzymatic activity of The Crystal Structure of Mouse PP1G in Complex with Truncated Human PPP1R15B (631-669)
All present enzymatic activity of The Crystal Structure of Mouse PP1G in Complex with Truncated Human PPP1R15B (631-669):
3.1.3.16;
Protein crystallography data
The structure of The Crystal Structure of Mouse PP1G in Complex with Truncated Human PPP1R15B (631-669), PDB code: 4v0w
was solved by
R.Chen,
Y.Yan,
A.C.Casado,
D.Ron,
R.J.Read,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
33.936 /
1.55
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
67.010,
67.860,
156.750,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
17.27 /
20.29
|
Manganese Binding Sites:
The binding sites of Manganese atom in the The Crystal Structure of Mouse PP1G in Complex with Truncated Human PPP1R15B (631-669)
(pdb code 4v0w). This binding sites where shown within
5.0 Angstroms radius around Manganese atom.
In total 4 binding sites of Manganese where determined in the
The Crystal Structure of Mouse PP1G in Complex with Truncated Human PPP1R15B (631-669), PDB code: 4v0w:
Jump to Manganese binding site number:
1;
2;
3;
4;
Manganese binding site 1 out
of 4 in 4v0w
Go back to
Manganese Binding Sites List in 4v0w
Manganese binding site 1 out
of 4 in the The Crystal Structure of Mouse PP1G in Complex with Truncated Human PPP1R15B (631-669)
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 1 of The Crystal Structure of Mouse PP1G in Complex with Truncated Human PPP1R15B (631-669) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mn301
b:12.2
occ:0.25
|
O
|
A:HOH302
|
1.6
|
19.4
|
0.8
|
O
|
A:HOH2115
|
2.0
|
41.9
|
1.0
|
OD2
|
A:ASP64
|
2.1
|
17.3
|
1.0
|
OD2
|
A:ASP92
|
2.1
|
13.6
|
1.0
|
NE2
|
A:HIS66
|
2.2
|
15.2
|
1.0
|
MN
|
A:MN303
|
3.0
|
13.5
|
0.8
|
CE1
|
A:HIS66
|
3.0
|
20.5
|
1.0
|
CG
|
A:ASP92
|
3.1
|
15.0
|
1.0
|
CG
|
A:ASP64
|
3.2
|
15.8
|
1.0
|
O
|
A:HOH2152
|
3.3
|
22.1
|
1.0
|
CD2
|
A:HIS66
|
3.3
|
16.8
|
1.0
|
CB
|
A:ASP92
|
3.6
|
11.2
|
1.0
|
OD1
|
A:ASP64
|
4.1
|
16.6
|
1.0
|
CB
|
A:ASP64
|
4.1
|
11.5
|
1.0
|
CD2
|
A:HIS125
|
4.1
|
12.7
|
1.0
|
OD1
|
A:ASP92
|
4.2
|
13.0
|
1.0
|
ND1
|
A:HIS66
|
4.2
|
15.8
|
1.0
|
O
|
A:HOH2176
|
4.2
|
36.7
|
1.0
|
NE2
|
A:HIS125
|
4.3
|
15.7
|
1.0
|
NE2
|
A:HIS173
|
4.4
|
12.3
|
1.0
|
CG
|
A:HIS66
|
4.4
|
13.7
|
1.0
|
CE2
|
A:PHE267
|
4.4
|
15.3
|
1.0
|
CE1
|
A:HIS173
|
4.4
|
13.3
|
1.0
|
OH
|
A:TYR272
|
4.5
|
33.8
|
1.0
|
O
|
A:HOH2312
|
4.5
|
42.8
|
1.0
|
O
|
A:HIS248
|
4.5
|
21.0
|
1.0
|
CA
|
A:HIS248
|
4.6
|
12.2
|
1.0
|
OD1
|
A:ASN124
|
4.7
|
13.9
|
1.0
|
ND1
|
A:HIS248
|
4.8
|
14.3
|
1.0
|
C
|
A:HIS248
|
4.9
|
15.8
|
1.0
|
|
Manganese binding site 2 out
of 4 in 4v0w
Go back to
Manganese Binding Sites List in 4v0w
Manganese binding site 2 out
of 4 in the The Crystal Structure of Mouse PP1G in Complex with Truncated Human PPP1R15B (631-669)
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 2 of The Crystal Structure of Mouse PP1G in Complex with Truncated Human PPP1R15B (631-669) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mn303
b:13.5
occ:0.77
|
OD1
|
A:ASN124
|
2.1
|
13.9
|
1.0
|
OD2
|
A:ASP92
|
2.2
|
13.6
|
1.0
|
O
|
A:HOH302
|
2.2
|
19.4
|
0.8
|
NE2
|
A:HIS173
|
2.2
|
12.3
|
1.0
|
ND1
|
A:HIS248
|
2.3
|
14.3
|
1.0
|
O
|
A:HOH2152
|
2.5
|
22.1
|
1.0
|
MN
|
A:MN301
|
3.0
|
12.2
|
0.2
|
CE1
|
A:HIS248
|
3.1
|
21.2
|
1.0
|
CE1
|
A:HIS173
|
3.2
|
13.3
|
1.0
|
CG
|
A:ASP92
|
3.2
|
15.0
|
1.0
|
CG
|
A:ASN124
|
3.2
|
12.4
|
1.0
|
CD2
|
A:HIS173
|
3.2
|
8.8
|
1.0
|
CG
|
A:HIS248
|
3.4
|
13.5
|
1.0
|
OD1
|
A:ASP92
|
3.5
|
13.0
|
1.0
|
ND2
|
A:ASN124
|
3.7
|
14.7
|
1.0
|
CA
|
A:HIS248
|
3.8
|
12.2
|
1.0
|
CB
|
A:HIS248
|
3.9
|
12.2
|
1.0
|
OD2
|
A:ASP64
|
4.0
|
17.3
|
1.0
|
O
|
A:HOH2115
|
4.1
|
41.9
|
1.0
|
CD2
|
A:HIS125
|
4.2
|
12.7
|
1.0
|
O
|
A:HIS248
|
4.2
|
21.0
|
1.0
|
NE2
|
A:HIS248
|
4.3
|
17.3
|
1.0
|
ND1
|
A:HIS173
|
4.3
|
10.2
|
1.0
|
CG
|
A:HIS173
|
4.4
|
9.3
|
1.0
|
CB
|
A:ASP92
|
4.4
|
11.2
|
1.0
|
CD2
|
A:HIS248
|
4.5
|
14.3
|
1.0
|
N
|
A:ASN124
|
4.5
|
10.3
|
1.0
|
CB
|
A:ASN124
|
4.5
|
11.1
|
1.0
|
C
|
A:HIS248
|
4.5
|
15.8
|
1.0
|
O
|
A:HOH2176
|
4.5
|
36.7
|
1.0
|
NE2
|
A:HIS125
|
4.8
|
15.7
|
1.0
|
N
|
A:HIS248
|
4.8
|
12.7
|
1.0
|
O
|
A:LEU205
|
4.8
|
12.1
|
1.0
|
CG
|
A:ASP64
|
4.8
|
15.8
|
1.0
|
OD1
|
A:ASP64
|
4.9
|
16.6
|
1.0
|
NE2
|
A:HIS66
|
5.0
|
15.2
|
1.0
|
CA
|
A:ASN124
|
5.0
|
10.4
|
1.0
|
|
Manganese binding site 3 out
of 4 in 4v0w
Go back to
Manganese Binding Sites List in 4v0w
Manganese binding site 3 out
of 4 in the The Crystal Structure of Mouse PP1G in Complex with Truncated Human PPP1R15B (631-669)
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 3 of The Crystal Structure of Mouse PP1G in Complex with Truncated Human PPP1R15B (631-669) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Mn301
b:10.4
occ:0.22
|
O
|
C:HOH302
|
1.9
|
16.0
|
0.8
|
O
|
C:HOH2066
|
2.0
|
40.8
|
1.0
|
NE2
|
C:HIS66
|
2.1
|
19.1
|
1.0
|
OD2
|
C:ASP64
|
2.1
|
16.0
|
1.0
|
OD2
|
C:ASP92
|
2.2
|
14.5
|
1.0
|
CE1
|
C:HIS66
|
2.9
|
20.2
|
1.0
|
MN
|
C:MN303
|
3.1
|
13.7
|
0.8
|
CD2
|
C:HIS66
|
3.2
|
16.7
|
1.0
|
CG
|
C:ASP92
|
3.2
|
13.9
|
1.0
|
CG
|
C:ASP64
|
3.3
|
14.6
|
1.0
|
O
|
C:HOH2092
|
3.4
|
17.0
|
1.0
|
CB
|
C:ASP92
|
3.7
|
10.8
|
1.0
|
O
|
C:HOH2195
|
3.9
|
37.0
|
1.0
|
CB
|
C:ASP64
|
4.1
|
12.9
|
1.0
|
CD2
|
C:HIS125
|
4.1
|
13.8
|
1.0
|
ND1
|
C:HIS66
|
4.1
|
19.8
|
1.0
|
OD1
|
C:ASP64
|
4.1
|
15.9
|
1.0
|
CG
|
C:HIS66
|
4.3
|
14.1
|
1.0
|
OD1
|
C:ASP92
|
4.3
|
13.5
|
1.0
|
NE2
|
C:HIS125
|
4.3
|
17.3
|
1.0
|
OH
|
C:TYR272
|
4.4
|
28.2
|
1.0
|
NE2
|
C:HIS173
|
4.5
|
12.9
|
1.0
|
CE1
|
C:PHE267
|
4.5
|
14.5
|
1.0
|
CE1
|
C:HIS173
|
4.5
|
17.6
|
1.0
|
O
|
C:HIS248
|
4.6
|
23.9
|
1.0
|
CA
|
C:HIS248
|
4.7
|
14.2
|
1.0
|
OD1
|
C:ASN124
|
4.8
|
15.3
|
1.0
|
ND1
|
C:HIS248
|
4.9
|
12.1
|
1.0
|
C
|
C:HIS248
|
4.9
|
16.1
|
1.0
|
|
Manganese binding site 4 out
of 4 in 4v0w
Go back to
Manganese Binding Sites List in 4v0w
Manganese binding site 4 out
of 4 in the The Crystal Structure of Mouse PP1G in Complex with Truncated Human PPP1R15B (631-669)
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 4 of The Crystal Structure of Mouse PP1G in Complex with Truncated Human PPP1R15B (631-669) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Mn303
b:13.7
occ:0.85
|
OD1
|
C:ASN124
|
2.2
|
15.3
|
1.0
|
OD2
|
C:ASP92
|
2.2
|
14.5
|
1.0
|
NE2
|
C:HIS173
|
2.2
|
12.9
|
1.0
|
O
|
C:HOH302
|
2.2
|
16.0
|
0.8
|
ND1
|
C:HIS248
|
2.3
|
12.1
|
1.0
|
O
|
C:HOH2092
|
2.4
|
17.0
|
1.0
|
CE1
|
C:HIS248
|
3.1
|
18.1
|
1.0
|
MN
|
C:MN301
|
3.1
|
10.4
|
0.2
|
CE1
|
C:HIS173
|
3.2
|
17.6
|
1.0
|
CG
|
C:ASP92
|
3.2
|
13.9
|
1.0
|
CD2
|
C:HIS173
|
3.2
|
12.4
|
1.0
|
CG
|
C:ASN124
|
3.2
|
14.2
|
1.0
|
CG
|
C:HIS248
|
3.4
|
11.2
|
1.0
|
OD1
|
C:ASP92
|
3.6
|
13.5
|
1.0
|
ND2
|
C:ASN124
|
3.7
|
15.0
|
1.0
|
CA
|
C:HIS248
|
3.7
|
14.2
|
1.0
|
CB
|
C:HIS248
|
3.9
|
12.1
|
1.0
|
OD2
|
C:ASP64
|
3.9
|
16.0
|
1.0
|
O
|
C:HOH2195
|
4.0
|
37.0
|
1.0
|
CD2
|
C:HIS125
|
4.1
|
13.8
|
1.0
|
O
|
C:HIS248
|
4.2
|
23.9
|
1.0
|
O
|
C:HOH2066
|
4.2
|
40.8
|
1.0
|
ND1
|
C:HIS173
|
4.3
|
12.6
|
1.0
|
NE2
|
C:HIS248
|
4.3
|
14.9
|
1.0
|
CG
|
C:HIS173
|
4.3
|
12.2
|
1.0
|
CB
|
C:ASP92
|
4.4
|
10.8
|
1.0
|
C
|
C:HIS248
|
4.5
|
16.1
|
1.0
|
CD2
|
C:HIS248
|
4.5
|
12.3
|
1.0
|
CB
|
C:ASN124
|
4.5
|
12.0
|
1.0
|
N
|
C:ASN124
|
4.5
|
12.6
|
1.0
|
NE2
|
C:HIS125
|
4.7
|
17.3
|
1.0
|
N
|
C:HIS248
|
4.7
|
11.0
|
1.0
|
O
|
C:LEU205
|
4.8
|
13.0
|
1.0
|
CG
|
C:ASP64
|
4.8
|
14.6
|
1.0
|
OD1
|
C:ASP64
|
4.9
|
15.9
|
1.0
|
NE2
|
C:HIS66
|
5.0
|
19.1
|
1.0
|
|
Reference:
R.Chen,
C.Rato,
Y.Yan,
A.Crespillo-Casado,
H.J.Clarke,
H.P.Harding,
S.J.Marciniak,
R.J.Read,
D.Ron.
G-Actin Provides Substrate-Specificity to Eukaryotic Initiation Factor 2ALPHA Holophosphatases. Elife V. 4 2015.
ISSN: ISSN 2050-084X
PubMed: 25774600
DOI: 10.7554/ELIFE.04871
Page generated: Sat Oct 5 21:29:33 2024
|