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Manganese in PDB 5vpu: Crystal Structure of 2,3-Bisphosphoglycerate-Independent Phosphoglycerate Mutase Bound to 3-Phosphoglycerate, From Acinetobacter Baumannii

Enzymatic activity of Crystal Structure of 2,3-Bisphosphoglycerate-Independent Phosphoglycerate Mutase Bound to 3-Phosphoglycerate, From Acinetobacter Baumannii

All present enzymatic activity of Crystal Structure of 2,3-Bisphosphoglycerate-Independent Phosphoglycerate Mutase Bound to 3-Phosphoglycerate, From Acinetobacter Baumannii:
5.4.2.12;

Protein crystallography data

The structure of Crystal Structure of 2,3-Bisphosphoglycerate-Independent Phosphoglycerate Mutase Bound to 3-Phosphoglycerate, From Acinetobacter Baumannii, PDB code: 5vpu was solved by Seattle Structural Genomics Center For Infectious Disease (Ssgcid), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 41.05 / 1.50
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 45.940, 82.090, 72.410, 90.00, 97.64, 90.00
R / Rfree (%) 13.5 / 16.4

Manganese Binding Sites:

The binding sites of Manganese atom in the Crystal Structure of 2,3-Bisphosphoglycerate-Independent Phosphoglycerate Mutase Bound to 3-Phosphoglycerate, From Acinetobacter Baumannii (pdb code 5vpu). 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 2,3-Bisphosphoglycerate-Independent Phosphoglycerate Mutase Bound to 3-Phosphoglycerate, From Acinetobacter Baumannii, PDB code: 5vpu:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in 5vpu

Go back to Manganese Binding Sites List in 5vpu
Manganese binding site 1 out of 2 in the Crystal Structure of 2,3-Bisphosphoglycerate-Independent Phosphoglycerate Mutase Bound to 3-Phosphoglycerate, From Acinetobacter Baumannii


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 2,3-Bisphosphoglycerate-Independent Phosphoglycerate Mutase Bound to 3-Phosphoglycerate, From Acinetobacter Baumannii within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn601

b:9.1
occ:1.00
 NE2 A:HIS407 2.0 7.8 1.0
NE2 A:HIS463 2.0 11.6 1.0
OD1 A:ASP403 2.1 12.9 1.0
O2P A:3PG603 2.4 44.5 1.0
O1P A:3PG603 2.4 35.1 1.0
OD2 A:ASP403 2.6 13.7 1.0
CG A:ASP403 2.7 12.6 1.0
P A:3PG603 2.9 26.2 1.0
CE1 A:HIS407 2.9 8.1 1.0
CD2 A:HIS407 3.0 10.4 1.0
CD2 A:HIS463 3.0 10.1 1.0
CE1 A:HIS463 3.0 10.9 1.0
C3 A:3PG603 3.4 16.2 1.0
O A:HOH729 3.6 13.0 1.0
O3P A:3PG603 3.8 16.2 1.0
CE1 A:HIS445 3.9 11.1 1.0
ND2 A:ASN447 4.0 10.2 1.0
ND1 A:HIS407 4.1 8.5 1.0
CG A:HIS407 4.1 8.4 1.0
O4P A:3PG603 4.1 18.6 1.0
CB A:ASP403 4.1 11.0 1.0
ND1 A:HIS463 4.1 10.4 1.0
CG A:HIS463 4.1 10.1 1.0
C2 A:3PG603 4.2 19.2 1.0
NE2 A:HIS445 4.2 13.0 1.0
O1 A:3PG603 4.4 19.2 1.0
MN A:MN602 4.4 11.8 0.9
NZ A:LYS336 4.5 15.2 1.0
C1 A:3PG603 4.6 13.4 1.0
O A:ASP403 4.7 10.7 1.0
OG A:SER67 4.7 22.7 1.0
CA A:ASP403 4.9 9.4 1.0
OD1 A:ASP17 4.9 13.5 1.0
C A:ASP403 4.9 9.8 1.0
O A:HOH1051 5.0 12.9 1.0
ND1 A:HIS445 5.0 10.7 1.0

Manganese binding site 2 out of 2 in 5vpu

Go back to Manganese Binding Sites List in 5vpu
Manganese binding site 2 out of 2 in the Crystal Structure of 2,3-Bisphosphoglycerate-Independent Phosphoglycerate Mutase Bound to 3-Phosphoglycerate, From Acinetobacter Baumannii


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 2,3-Bisphosphoglycerate-Independent Phosphoglycerate Mutase Bound to 3-Phosphoglycerate, From Acinetobacter Baumannii within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn602

b:11.8
occ:0.88
 OG A:SER67 1.9 22.7 1.0
OD1 A:ASP17 1.9 13.5 1.0
NE2 A:HIS445 2.0 13.0 1.0
OD2 A:ASP444 2.3 21.7 1.0
O2P A:3PG603 2.7 44.5 1.0
CG A:ASP17 2.7 14.6 1.0
CD2 A:HIS445 2.9 11.3 1.0
OD2 A:ASP17 2.9 15.8 1.0
CE1 A:HIS445 3.0 11.1 1.0
CB A:SER67 3.1 22.3 1.0
CG A:ASP444 3.2 14.8 1.0
OD1 A:ASP444 3.3 18.9 1.0
CA A:SER67 3.5 15.2 1.0
N A:SER67 3.7 11.9 1.0
P A:3PG603 3.9 26.2 1.0
NZ A:LYS336 3.9 15.2 1.0
O3P A:3PG603 3.9 16.2 1.0
OD1 A:ASP403 4.1 12.9 1.0
ND1 A:HIS445 4.1 10.7 1.0
CG A:HIS445 4.1 9.4 1.0
CG A:ASP403 4.1 12.6 1.0
CB A:ASP17 4.1 10.7 1.0
OD2 A:ASP403 4.4 13.7 1.0
N A:GLY18 4.4 11.1 1.0
MN A:MN601 4.4 9.1 1.0
C A:ASN66 4.4 12.8 1.0
O4P A:3PG603 4.5 18.6 1.0
CB A:ASP444 4.5 18.8 1.0
CB A:ASP403 4.5 11.0 1.0
CA A:ASP17 4.6 10.7 1.0
CE1 A:HIS463 4.6 10.9 1.0
NE2 A:HIS463 4.7 11.6 1.0
C A:ASP17 4.8 10.6 1.0
CD2 A:HIS339 4.9 28.3 1.0
CE1 A:HIS71 4.9 14.5 1.0
C A:SER67 5.0 13.5 1.0

Reference:

S.L.Delker, D.D.Drannow, J.Abendroth, D.Lorimer, T.E.Edwards, Seattle Structural Genomics Center For Infectious Disease(Ssgcid). Crystal Structure of 2,3-Bisphosphoglycerate-Independent Phosphoglycerate Mutase Bound to 3-Phosphoglycerate, From Acinetobacter Baumannii To Be Published.
Page generated: Sun Oct 6 03:12:08 2024

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