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Manganese in PDB 4qax: Crystal Structure of Post-Catalytic Binary Complex of Phosphoglycerate Mutase From Staphylococcus Aureus

Enzymatic activity of Crystal Structure of Post-Catalytic Binary Complex of Phosphoglycerate Mutase From Staphylococcus Aureus

All present enzymatic activity of Crystal Structure of Post-Catalytic Binary Complex of Phosphoglycerate Mutase From Staphylococcus Aureus:
5.4.2.12;

Protein crystallography data

The structure of Crystal Structure of Post-Catalytic Binary Complex of Phosphoglycerate Mutase From Staphylococcus Aureus, PDB code: 4qax 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) 19.53 / 2.00
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 72.802, 80.689, 89.254, 90.00, 90.00, 90.00
R / Rfree (%) 16.6 / 21.4

Manganese Binding Sites:

The binding sites of Manganese atom in the Crystal Structure of Post-Catalytic Binary Complex of Phosphoglycerate Mutase From Staphylococcus Aureus (pdb code 4qax). 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 Post-Catalytic Binary Complex of Phosphoglycerate Mutase From Staphylococcus Aureus, PDB code: 4qax:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in 4qax

Go back to Manganese Binding Sites List in 4qax
Manganese binding site 1 out of 2 in the Crystal Structure of Post-Catalytic Binary Complex of Phosphoglycerate Mutase From Staphylococcus Aureus


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 Post-Catalytic Binary Complex of Phosphoglycerate Mutase From Staphylococcus Aureus within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn601

b:15.9
occ:1.00
O A:HOH702 2.1 16.0 1.0
OD1 A:ASP397 2.1 15.1 1.0
O A:HOH703 2.1 17.5 1.0
O A:HOH701 2.2 16.4 1.0
NE2 A:HIS401 2.2 17.9 1.0
NE2 A:HIS456 2.4 19.0 1.0
CG A:ASP397 3.0 16.4 1.0
CD2 A:HIS401 3.2 17.1 1.0
OD2 A:ASP397 3.2 14.3 1.0
CE1 A:HIS401 3.2 16.8 1.0
CE1 A:HIS456 3.2 19.1 1.0
CD2 A:HIS456 3.4 17.5 1.0
NZ A:LYS330 4.0 16.0 1.0
ND1 A:HIS401 4.3 19.7 1.0
O A:HOH842 4.3 26.2 1.0
CG A:HIS401 4.3 18.0 1.0
O A:HOH806 4.4 21.3 1.0
O A:HOH729 4.4 19.6 1.0
ND1 A:HIS456 4.4 17.7 1.0
OG A:SER62 4.5 13.9 1.0
CB A:ASP397 4.5 15.2 1.0
CE1 A:HIS439 4.5 15.3 1.0
CG A:HIS456 4.5 17.7 1.0
ND2 A:ASN441 4.7 16.2 1.0
O A:HOH867 4.8 32.1 1.0
NE2 A:HIS439 4.8 16.5 1.0
SD A:MET398 4.9 18.5 1.0

Manganese binding site 2 out of 2 in 4qax

Go back to Manganese Binding Sites List in 4qax
Manganese binding site 2 out of 2 in the Crystal Structure of Post-Catalytic Binary Complex of Phosphoglycerate Mutase From Staphylococcus Aureus


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 Post-Catalytic Binary Complex of Phosphoglycerate Mutase From Staphylococcus Aureus within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn602

b:9.7
occ:1.00
OD1 A:ASP12 1.9 13.9 1.0
OG A:SER62 1.9 13.9 1.0
OD1 A:ASP438 2.0 14.6 1.0
NE2 A:HIS439 2.1 16.5 1.0
CG A:ASP12 2.6 14.2 1.0
CG A:ASP438 2.7 13.8 1.0
OD2 A:ASP12 2.8 14.5 1.0
OD2 A:ASP438 2.9 15.8 1.0
CD2 A:HIS439 2.9 15.0 1.0
CB A:SER62 3.1 13.7 1.0
CE1 A:HIS439 3.2 15.3 1.0
CA A:SER62 3.3 14.5 1.0
N A:SER62 3.7 14.5 1.0
NZ A:LYS330 3.8 16.0 1.0
CB A:ASP12 4.0 13.9 1.0
CG A:HIS439 4.1 15.6 1.0
O A:HOH702 4.1 16.0 1.0
OD1 A:ASP397 4.1 15.1 1.0
ND1 A:HIS439 4.2 16.4 1.0
CB A:ASP438 4.2 13.0 1.0
N A:GLY13 4.3 13.9 1.0
C A:ASN61 4.3 14.8 1.0
CG A:ASP397 4.3 16.4 1.0
CA A:ASP12 4.5 14.5 1.0
CE A:LYS330 4.5 15.4 1.0
CE1 A:HIS66 4.5 16.5 1.0
O A:ASN61 4.6 14.6 1.0
C A:SER62 4.7 14.5 1.0
OD2 A:ASP397 4.7 14.3 1.0
CB A:ASP397 4.7 15.2 1.0
C A:ASP12 4.7 14.6 1.0
ND1 A:HIS66 4.8 16.4 1.0
CD A:LYS330 4.9 16.4 1.0

Reference:

A.Roychowdhury, A.Kundu, M.Bose, A.Gujar, S.Mukherjee, A.K.Das. Structural and Funcctional Analysis of Phosphoglycerate Mutase From Staphylococcus Aureus To Be Published.
Page generated: Tue Dec 15 04:27:41 2020

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