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Zinc in PDB 5zvx: Crystal Structure of K86A Mutant of Phosphomannose Isomerase From Salmonella Typhimurium

Enzymatic activity of Crystal Structure of K86A Mutant of Phosphomannose Isomerase From Salmonella Typhimurium

All present enzymatic activity of Crystal Structure of K86A Mutant of Phosphomannose Isomerase From Salmonella Typhimurium:
5.3.1.8;

Protein crystallography data

The structure of Crystal Structure of K86A Mutant of Phosphomannose Isomerase From Salmonella Typhimurium, PDB code: 5zvx was solved by M.Bangera, M.R.N.Murthy, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.58 / 1.70
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 36.190, 91.730, 116.660, 90.00, 90.00, 90.00
R / Rfree (%) 16.4 / 20.6

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of K86A Mutant of Phosphomannose Isomerase From Salmonella Typhimurium (pdb code 5zvx). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Crystal Structure of K86A Mutant of Phosphomannose Isomerase From Salmonella Typhimurium, PDB code: 5zvx:

Zinc binding site 1 out of 1 in 5zvx

Go back to Zinc Binding Sites List in 5zvx
Zinc binding site 1 out of 1 in the Crystal Structure of K86A Mutant of Phosphomannose Isomerase From Salmonella Typhimurium


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of K86A Mutant of Phosphomannose Isomerase From Salmonella Typhimurium within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn401

b:13.0
occ:0.70
 O A:HOH503 1.5 16.9 1.0
OE1 A:GLU134 2.0 15.8 1.0
NE2 A:HIS255 2.1 9.5 1.0
NE2 A:HIS99 2.2 13.0 1.0
CD A:GLU134 2.8 16.3 1.0
OE2 A:GLU134 3.0 15.2 1.0
CE1 A:HIS255 3.0 9.2 1.0
CD2 A:HIS99 3.0 12.8 1.0
CD2 A:HIS255 3.2 10.0 1.0
CE1 A:HIS99 3.3 13.6 1.0
O1 A:EDO407 3.5 27.6 1.0
O A:HOH714 3.9 43.3 1.0
OE1 A:GLN97 3.9 17.0 1.0
OH A:TYR257 3.9 14.5 1.0
C1 A:EDO407 3.9 23.4 1.0
CG A:GLU134 4.1 12.9 1.0
ND1 A:HIS255 4.2 10.1 1.0
CG A:HIS99 4.2 11.7 1.0
O A:HOH572 4.3 43.3 1.0
CG A:HIS255 4.3 8.7 1.0
ND1 A:HIS99 4.3 14.3 1.0
CB A:GLN97 4.5 11.2 1.0
CZ A:TYR257 4.5 13.2 1.0
OE1 A:GLU264 4.7 13.1 0.5
CD A:GLN97 4.8 14.4 1.0
CB A:GLU134 4.8 10.7 1.0
CE2 A:TYR257 4.9 12.6 1.0
CB A:LEU249 4.9 9.3 1.0
CG A:LEU249 4.9 9.4 1.0

Reference:

M.Bangera, G.Gowda K, S.R.Sagurthi, M.R.N.Murthy. Structural and Functional Insights Into Phosphomannose Isomerase: the Role of Zinc and Catalytic Residues. Acta Crystallogr D Struct V. 75 475 2019BIOL.
ISSN: ISSN 2059-7983
PubMed: 31063150
DOI: 10.1107/S2059798319004169
Page generated: Mon Oct 28 17:11:24 2024

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