PDBsum entry 3u96

Hydrolase

PDB id: 3u96

Contents

Protein chains

282 a.a.

Ligands

CSN ×2

SO4 ×2

Waters ×309

PDB id:

3u96

Name:

Hydrolase

Title:

Crystal structure of yophq357f(catalytic domain, residues 163-468) in complex with pncs

Structure:

Tyrosine-protein phosphatase yoph. Chain: a, b. Fragment: unp residues 163-468. Synonym: virulence protein. Engineered: yes. Mutation: yes

Source:

Yersinia enterocolitica. Organism_taxid: 630. Gene: yop51, yoph. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

1.80Å R-factor: 0.181 R-free: 0.207

Authors:

M.C.Ho,S.Ke

Key ref:

S.Ke et al. (2012). Investigation of catalytic loop structure, dynamics, and function relationship of Yersinia protein tyrosine phosphatase by temperature-jump relaxation spectroscopy and X-ray structural determination. J Phys Chem B, 116, 6166-6176. PubMed id: 22564106

Date:

17-Oct-11 Release date: 29-Aug-12

Protein chains

P15273  (YOPH_YEREN) -  Tyrosine-protein phosphatase YopH from Yersinia enterocolitica

Seq: 468 a.a.

Struc: 282 a.a.*

* PDB and UniProt seqs differ at 2 residue positions (black crosses)

Enzyme reactions

• Enzyme class: E.C.3.1.3.48 - protein-tyrosine-phosphatase.
• Reaction: O-phospho-L-tyrosyl-[protein] + H2O = L-tyrosyl-[protein] + phosphate

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

Key reference

J Phys Chem B 116:6166-6176 (2012)

PubMed id: 22564106

Investigation of catalytic loop structure, dynamics, and function relationship of Yersinia protein tyrosine phosphatase by temperature-jump relaxation spectroscopy and X-ray structural determination.

S.Ke, M.C.Ho, N.Zhadin, H.Deng, R.Callender.

ABSTRACT

No abstract given.