› 3u96

X-ray diffraction
1.8Å resolution

Crystal Structure of YopHQ357F(Catalytic Domain, Residues 163-468) in complex with pNCS

Released:
DOI: 10.2210/pdb3u96/pdb
Model geometry
Fit model/data
PDB entry 3u96 coloured by chain, front view.
PDB entry 3u96 coloured by chain, side view.
PDB entry 3u96 coloured by chain, top view.
Source organism: Yersinia enterocolitica
Primary publication:
Investigation of catalytic loop structure, dynamics, and function relationship of Yersinia protein tyrosine phosphatase by temperature-jump relaxation spectroscopy and X-ray structural determination.
Ke S, Ho MC, Zhadin N, Deng H, Callender R
J Phys Chem B 116 6166-76 (2012)
PMID: 22564106

Function and Biology Details

Reaction catalysed: 
Protein tyrosine phosphate + H(2)O = protein tyrosine + phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assemblies composition:
homo dimer
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-147287 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tyrosine-protein phosphatase YopH Chains: A, B
Molecule details ›
Chains: A, B
Length: 306 amino acids
Theoretical weight: 33.54 KDa
Source organism: Yersinia enterocolitica
Expression system: Escherichia coli
UniProt:
  • Canonical: P15273 (Residues: 163-468; Coverage: 65%)
Gene names: yop51, yopH
Sequence domains: Protein-tyrosine phosphatase
Structure domains: Protein tyrosine phosphatase superfamily

Ligands and Environments

2 bound ligands:
Ligand CSN 2 x CSN
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: NSLS BEAMLINE X29A
Spacegroup: P1
Unit cell:
a: 49.863Å b: 53.993Å c: 65.759Å
α: 104.78° β: 108.79° γ: 97.83°
R-values:
R R work R free
0.181 0.179 0.207
Expression system: Escherichia coli

Quick links

Citations

3 citation in other articles

Loop Dynamics and Enzyme Catalysis in Protein Tyrosine Phosphatases.
Crean et al. (2021)
2 more

2 mentions without citation

Investigation of catalytic loop structure, dynamics, and function relationship of Yersinia protein tyrosine phosphatase by temperature-jump relaxation spectroscopy and X-ray structural determination.
Ke et al. (2012)
1 more

PDB-REDO

The sliders below show the change in model quality between original PDB entry and the PDB-REDO entry

Model Geometry
 
 
Data not available
DNA/RNA Geometry
 
 
Data not available
Fit model/data
 
 
Data not available
PDB-REDO