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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

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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

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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

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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

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