Atomistry » Zinc » PDB 5zn8-6a12 » 5zvu
Atomistry »
  Zinc »
    PDB 5zn8-6a12 »
      5zvu »

Zinc in PDB 5zvu: Crystal Structure of K132A Mutant of Phosphomannose Isomerase From Salmonella Typhimurium

Enzymatic activity of Crystal Structure of K132A Mutant of Phosphomannose Isomerase From Salmonella Typhimurium

All present enzymatic activity of Crystal Structure of K132A Mutant of Phosphomannose Isomerase From Salmonella Typhimurium:
5.3.1.8;

Protein crystallography data

The structure of Crystal Structure of K132A Mutant of Phosphomannose Isomerase From Salmonella Typhimurium, PDB code: 5zvu 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) 37.23 / 2.20
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 36.140, 91.790, 111.690, 90.00, 90.00, 90.00
R / Rfree (%) 21.3 / 27.3

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of K132A Mutant of Phosphomannose Isomerase From Salmonella Typhimurium (pdb code 5zvu). 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 K132A Mutant of Phosphomannose Isomerase From Salmonella Typhimurium, PDB code: 5zvu:

Zinc binding site 1 out of 1 in 5zvu

Go back to Zinc Binding Sites List in 5zvu
Zinc binding site 1 out of 1 in the Crystal Structure of K132A 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 K132A Mutant of Phosphomannose Isomerase From Salmonella Typhimurium within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn401

b:53.9
occ:1.00
 NE2 A:HIS255 2.2 16.9 1.0
O1 A:EDO402 2.6 39.9 1.0
NE2 A:HIS99 2.7 23.9 1.0
OE1 A:GLU134 2.9 28.8 1.0
CD2 A:HIS255 3.2 16.1 1.0
CE1 A:HIS255 3.2 17.3 1.0
CD A:GLU134 3.4 27.2 1.0
O A:HOH508 3.4 24.5 1.0
CE1 A:HIS99 3.5 23.9 1.0
CD2 A:HIS99 3.6 23.4 1.0
OE2 A:GLU134 3.6 28.8 1.0
C1 A:EDO402 3.7 35.2 1.0
OE1 A:GLN97 3.8 20.8 1.0
OH A:TYR257 4.2 19.4 1.0
O A:HOH560 4.3 20.2 1.0
ND1 A:HIS255 4.3 17.5 1.0
CG A:HIS255 4.3 16.2 1.0
CG A:GLU134 4.5 23.6 1.0
CZ A:TYR257 4.6 18.6 1.0
ND1 A:HIS99 4.6 24.2 1.0
CB A:GLN97 4.6 18.1 1.0
CD1 A:LEU249 4.6 15.6 1.0
CG A:HIS99 4.7 23.0 1.0
CB A:GLU134 4.7 22.3 1.0
CD A:GLN97 4.8 19.7 1.0
C2 A:EDO402 4.9 32.2 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

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy