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Manganese in PDB 4nwx: Crystal Structure of Phosphoglycerate Mutase From Staphylococcus Aureus in 2-Phosphoglyceric Acid Bound Form

Enzymatic activity of Crystal Structure of Phosphoglycerate Mutase From Staphylococcus Aureus in 2-Phosphoglyceric Acid Bound Form

All present enzymatic activity of Crystal Structure of Phosphoglycerate Mutase From Staphylococcus Aureus in 2-Phosphoglyceric Acid Bound Form:
5.4.2.12;

Protein crystallography data

The structure of Crystal Structure of Phosphoglycerate Mutase From Staphylococcus Aureus in 2-Phosphoglyceric Acid Bound Form, PDB code: 4nwx was solved by A.Roychowdhury, A.Kundu, M.Bose, A.Gujar, A.K.Das, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.64 / 2.01
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 73.639, 83.206, 89.073, 90.00, 90.00, 90.00
R / Rfree (%) 16.8 / 21.6

Manganese Binding Sites:

The binding sites of Manganese atom in the Crystal Structure of Phosphoglycerate Mutase From Staphylococcus Aureus in 2-Phosphoglyceric Acid Bound Form (pdb code 4nwx). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Crystal Structure of Phosphoglycerate Mutase From Staphylococcus Aureus in 2-Phosphoglyceric Acid Bound Form, PDB code: 4nwx:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in 4nwx

Go back to Manganese Binding Sites List in 4nwx
Manganese binding site 1 out of 2 in the Crystal Structure of Phosphoglycerate Mutase From Staphylococcus Aureus in 2-Phosphoglyceric Acid Bound Form


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 Phosphoglycerate Mutase From Staphylococcus Aureus in 2-Phosphoglyceric Acid Bound Form within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn602

b:8.3
occ:1.00
OD1 A:ASP12 1.8 12.9 1.0
OG A:SER62 1.9 11.6 1.0
OD2 A:ASP438 2.0 11.0 1.0
NE2 A:HIS439 2.1 13.9 1.0
CG A:ASP12 2.5 12.5 1.0
OD2 A:ASP12 2.7 11.7 1.0
CG A:ASP438 2.7 12.2 1.0
OD1 A:ASP438 2.9 11.5 1.0
CD2 A:HIS439 2.9 12.7 1.0
CB A:SER62 3.0 11.3 1.0
CE1 A:HIS439 3.1 14.3 1.0
CA A:SER62 3.3 11.6 1.0
N A:SER62 3.7 12.5 1.0
NZ A:LYS330 3.7 11.6 1.0
CB A:ASP12 3.9 12.3 1.0
CG A:HIS439 4.1 13.3 1.0
ND1 A:HIS439 4.1 13.0 1.0
OD1 A:ASP397 4.2 11.7 1.0
CB A:ASP438 4.2 12.2 1.0
CE A:LYS330 4.2 11.1 1.0
CG A:ASP397 4.3 13.3 1.0
C A:ASN61 4.3 12.0 1.0
N A:GLY13 4.3 11.2 1.0
O A:HOH1002 4.3 19.5 1.0
CA A:ASP12 4.4 11.6 1.0
CE1 A:HIS66 4.5 11.1 1.0
OD2 A:ASP397 4.6 12.3 1.0
C A:SER62 4.7 11.7 1.0
C A:ASP12 4.7 12.0 1.0
O A:ASN61 4.7 11.2 1.0
CB A:ASP397 4.7 12.7 1.0
CD A:LYS330 4.8 10.9 1.0
ND1 A:HIS66 4.9 11.7 1.0

Manganese binding site 2 out of 2 in 4nwx

Go back to Manganese Binding Sites List in 4nwx
Manganese binding site 2 out of 2 in the Crystal Structure of Phosphoglycerate Mutase From Staphylococcus Aureus in 2-Phosphoglyceric Acid Bound Form


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 Phosphoglycerate Mutase From Staphylococcus Aureus in 2-Phosphoglyceric Acid Bound Form within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn603

b:13.7
occ:1.00
OD1 A:ASP397 2.1 11.7 1.0
O A:HOH1004 2.1 30.4 1.0
O A:HOH1002 2.1 19.5 1.0
NE2 A:HIS401 2.2 15.1 1.0
O A:HOH1003 2.2 34.0 1.0
NE2 A:HIS456 2.2 14.9 1.0
CG A:ASP397 2.9 13.3 1.0
OD2 A:ASP397 3.0 12.3 1.0
CE1 A:HIS401 3.1 14.7 1.0
CE1 A:HIS456 3.1 16.0 1.0
CD2 A:HIS401 3.2 14.1 1.0
CD2 A:HIS456 3.3 15.1 1.0
NZ A:LYS330 4.0 11.6 1.0
ND1 A:HIS401 4.2 14.6 1.0
ND1 A:HIS456 4.3 15.2 1.0
CG A:HIS401 4.3 14.2 1.0
CB A:ASP397 4.3 12.7 1.0
CG A:HIS456 4.4 16.4 1.0
O A:HOH711 4.4 21.5 1.0
CE1 A:HIS439 4.4 14.3 1.0
OG A:SER62 4.5 11.6 1.0
ND2 A:ASN441 4.5 14.2 1.0
O A:HOH713 4.6 20.5 1.0
NE2 A:HIS439 4.8 13.9 1.0
SD A:MET398 4.8 15.2 1.0
O A:ASP397 5.0 12.8 1.0

Reference:

A.Roychowdhury, A.Kundu, M.Bose, A.Gujar, S.Mukherjee, A.K.Das. Complete Catalytic Cycle of Cofactor-Independent Phosphoglycerate Mutase Involves A Spring-Loaded Mechanism Febs J. 2015.
ISSN: ISSN 1742-464X
PubMed: 25611430
DOI: 10.1111/FEBS.13205
Page generated: Tue Dec 15 04:25:26 2020

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