Atomistry » Manganese » PDB 5z2k-6a9u » 5zqv
Atomistry »
  Manganese »
    PDB 5z2k-6a9u »
      5zqv »

Manganese in PDB 5zqv: Crystal Structure of Protein Phosphate 1 Complexed with PP1 Binding Domain of Gm

Enzymatic activity of Crystal Structure of Protein Phosphate 1 Complexed with PP1 Binding Domain of Gm

All present enzymatic activity of Crystal Structure of Protein Phosphate 1 Complexed with PP1 Binding Domain of Gm:
3.1.3.16;

Protein crystallography data

The structure of Crystal Structure of Protein Phosphate 1 Complexed with PP1 Binding Domain of Gm, PDB code: 5zqv 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) 33.29 / 2.95
Space group P 41
Cell size a, b, c (Å), α, β, γ (°) 111.973, 111.973, 195.299, 90.00, 90.00, 90.00
R / Rfree (%) 25.2 / 29.7

Manganese Binding Sites:

The binding sites of Manganese atom in the Crystal Structure of Protein Phosphate 1 Complexed with PP1 Binding Domain of Gm (pdb code 5zqv). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 4 binding sites of Manganese where determined in the Crystal Structure of Protein Phosphate 1 Complexed with PP1 Binding Domain of Gm, PDB code: 5zqv:
Jump to Manganese binding site number: 1; 2; 3; 4;

Manganese binding site 1 out of 4 in 5zqv

Go back to Manganese Binding Sites List in 5zqv
Manganese binding site 1 out of 4 in the Crystal Structure of Protein Phosphate 1 Complexed with PP1 Binding Domain of Gm


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 Gm within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn401

b:79.8
occ:1.00
NE2 A:HIS173 2.1 90.3 1.0
OD1 A:ASN124 2.1 92.0 1.0
ND1 A:HIS248 2.1 0.0 1.0
OD2 A:ASP92 2.5 0.7 1.0
CE1 A:HIS248 2.9 0.3 1.0
OA2 A:FLC402 3.0 55.8 1.0
CE1 A:HIS173 3.0 72.0 1.0
CG A:ASN124 3.0 91.8 1.0
CD2 A:HIS173 3.0 92.1 1.0
CG A:ASP92 3.2 86.7 1.0
CG A:HIS248 3.2 80.4 1.0
OD1 A:ASP92 3.4 76.7 1.0
ND2 A:ASN124 3.5 57.8 1.0
CA A:HIS248 3.5 93.9 1.0
CB A:HIS248 3.7 90.0 1.0
OD2 A:ASP64 4.0 80.0 1.0
CAC A:FLC402 4.1 99.9 1.0
NE2 A:HIS248 4.1 94.0 1.0
ND1 A:HIS173 4.1 58.3 1.0
O A:HIS248 4.1 81.6 1.0
CG A:HIS173 4.2 78.5 1.0
CD2 A:HIS248 4.3 80.9 1.0
CB A:ASN124 4.3 56.7 1.0
C A:HIS248 4.3 89.9 1.0
CD2 A:HIS125 4.4 89.2 1.0
N A:ASN124 4.5 77.3 1.0
CB A:ASP92 4.5 79.9 1.0
O A:LEU205 4.5 90.6 1.0
N A:HIS248 4.5 88.6 1.0
OA1 A:FLC402 4.5 0.6 1.0
CG A:ASP64 4.9 81.0 1.0
CA A:ASN124 4.9 81.8 1.0

Manganese binding site 2 out of 4 in 5zqv

Go back to Manganese Binding Sites List in 5zqv
Manganese binding site 2 out of 4 in the Crystal Structure of Protein Phosphate 1 Complexed with PP1 Binding Domain of Gm


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 Gm within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn401

b:90.4
occ:0.97
ND1 B:HIS248 2.0 0.8 1.0
OD2 B:ASP92 2.3 0.9 1.0
OD1 B:ASN124 2.4 67.6 1.0
CE1 B:HIS248 2.4 0.5 1.0
NE2 B:HIS173 2.8 70.3 1.0
CG B:ASN124 3.2 67.0 1.0
CG B:ASP92 3.2 89.2 1.0
ND2 B:ASN124 3.2 66.7 1.0
CG B:HIS248 3.2 0.7 1.0
CE1 B:HIS173 3.4 71.1 1.0
OD1 B:ASP92 3.4 72.1 1.0
NE2 B:HIS248 3.6 0.1 1.0
CD2 B:HIS125 3.8 80.8 1.0
CA B:HIS248 3.9 84.9 1.0
CD2 B:HIS173 4.0 71.2 1.0
CB B:HIS248 4.0 77.9 1.0
CD2 B:HIS248 4.0 77.5 1.0
O B:HIS248 4.2 0.0 1.0
OD2 B:ASP64 4.2 1.0 1.0
NE2 B:HIS125 4.4 73.7 1.0
C B:HIS248 4.5 0.2 1.0
CB B:ASP92 4.6 90.1 1.0
CB B:ASN124 4.6 66.9 1.0
ND1 B:HIS173 4.7 72.4 1.0
CE1 B:HIS66 4.8 93.0 1.0
NE2 B:HIS66 4.8 0.0 1.0
N B:ASN124 5.0 96.8 1.0
CG B:HIS173 5.0 72.5 1.0

Manganese binding site 3 out of 4 in 5zqv

Go back to Manganese Binding Sites List in 5zqv
Manganese binding site 3 out of 4 in the Crystal Structure of Protein Phosphate 1 Complexed with PP1 Binding Domain of Gm


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 Gm within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mn401

b:78.4
occ:0.91
ND1 C:HIS248 2.3 0.3 1.0
OD1 C:ASN124 2.4 88.1 1.0
OD2 C:ASP92 2.7 0.2 1.0
NE2 C:HIS173 2.8 79.0 1.0
CE1 C:HIS248 2.8 0.2 1.0
OA1 C:FLC402 3.0 0.6 1.0
CG C:ASN124 3.1 87.0 1.0
ND2 C:ASN124 3.1 86.1 1.0
CG C:ASP92 3.6 99.9 1.0
CG C:HIS248 3.6 0.9 1.0
CE1 C:HIS173 3.6 87.6 1.0
OD1 C:ASP92 3.7 90.4 1.0
CD2 C:HIS173 3.8 95.1 1.0
CD2 C:HIS125 3.9 0.1 1.0
CA C:HIS248 4.0 0.2 1.0
NE2 C:HIS248 4.1 0.1 1.0
CAC C:FLC402 4.2 0.4 1.0
O C:HIS248 4.2 0.2 1.0
CB C:HIS248 4.3 0.8 1.0
NE2 C:HIS125 4.4 0.9 1.0
OD2 C:ASP64 4.5 0.3 1.0
CD2 C:HIS248 4.5 0.9 1.0
CB C:ASN124 4.6 86.8 1.0
C C:HIS248 4.6 0.5 1.0
OHB C:FLC402 4.6 0.1 1.0
ND1 C:HIS173 4.8 97.5 1.0
OA2 C:FLC402 4.9 0.1 1.0
NH1 C:ARG221 4.9 0.2 1.0
CG C:HIS173 4.9 0.0 1.0
CB C:ASP92 5.0 0.0 1.0
CG C:HIS125 5.0 91.4 1.0

Manganese binding site 4 out of 4 in 5zqv

Go back to Manganese Binding Sites List in 5zqv
Manganese binding site 4 out of 4 in the Crystal Structure of Protein Phosphate 1 Complexed with PP1 Binding Domain of Gm


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 Gm within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mn401

b:95.6
occ:0.98
ND1 D:HIS248 2.1 0.9 1.0
OD1 D:ASN124 2.2 83.9 1.0
NE2 D:HIS173 2.3 98.5 1.0
OD2 D:ASP92 2.4 0.8 1.0
CE1 D:HIS248 2.9 0.5 1.0
OA1 D:FLC402 2.9 75.0 1.0
CE1 D:HIS173 3.1 91.2 1.0
CG D:HIS248 3.1 0.7 1.0
CG D:ASN124 3.1 82.3 1.0
CG D:ASP92 3.1 99.9 1.0
OD1 D:ASP92 3.3 87.1 1.0
ND2 D:ASN124 3.3 80.8 1.0
CD2 D:HIS173 3.5 0.6 1.0
CA D:HIS248 3.5 0.7 1.0
CB D:HIS248 3.5 0.1 1.0
CAC D:FLC402 3.8 98.8 1.0
OD2 D:ASP64 3.9 0.8 1.0
OA2 D:FLC402 4.0 0.8 1.0
NE2 D:HIS248 4.0 0.3 1.0
CD2 D:HIS248 4.1 97.8 1.0
CD2 D:HIS125 4.2 92.8 1.0
ND1 D:HIS173 4.3 93.7 1.0
O D:HIS248 4.3 0.9 1.0
C D:HIS248 4.4 0.8 1.0
CB D:ASP92 4.5 0.7 1.0
N D:HIS248 4.5 0.5 1.0
CG D:HIS173 4.5 0.6 1.0
CB D:ASN124 4.5 82.3 1.0
N D:ASN124 4.8 84.2 1.0
NE2 D:HIS125 4.8 77.2 1.0
CG D:ASP64 4.9 0.5 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 03:44:33 2024

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy