PDBsum entry 2y2f

Hydrolase

PDB id: 2y2f

Contents

Protein chain

282 a.a.

Ligands

YI1

Waters ×274

PDB id:

2y2f

Name:

Hydrolase

Title:

Crystal structure of yersinia pestis yoph in complex with an aminooxy- containing platform compound for inhibitor design

Structure:

Protein-tyrosine phosphatase yoph. Chain: a. Fragment: ptpase domain, residues 164-468. Synonym: uncharacterized protein yoph, uncharacterized protein ypcd1.67c. Engineered: yes

Source:

Yersinia pestis. Organism_taxid: 632. Expressed in: escherichia coli. Expression_system_taxid: 469008.

Resolution:

1.78Å R-factor: 0.167 R-free: 0.210

Authors:

G.T.Lountos,M.Bahta,B.Dyas,R.G.Ulrich,D.S.Waugh,T.R.Burke

Key ref:

M.Bahta et al. (2011). Utilization of nitrophenylphosphates and oxime-based ligation for the development of nanomolar affinity inhibitors of the Yersinia pestis outer protein H (YopH) phosphatase. J Med Chem, 54, 2933-2943. PubMed id: 21443195

Date:

14-Dec-10 Release date: 16-Mar-11

Protein chain

O68720  (O68720_YERPE) -  protein-tyrosine-phosphatase from Yersinia pestis

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 Med Chem 54:2933-2943 (2011)

PubMed id: 21443195

Utilization of nitrophenylphosphates and oxime-based ligation for the development of nanomolar affinity inhibitors of the Yersinia pestis outer protein H (YopH) phosphatase.

M.Bahta, G.T.Lountos, B.Dyas, S.E.Kim, R.G.Ulrich, D.S.Waugh, T.R.Burke.

ABSTRACT

No abstract given.