PDBsum entry 3zv2

Hydrolase

PDB id

3zv2

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Contents

			Protein chain

					281 a.a.

PDB id:

3zv2

Links

Name:

Hydrolase

Title:

Human protein-tyrosine phosphatase 1b c215a, s216a mutant

Structure:

Tyrosine-protein phosphatase non-receptor type 1. Chain: a. Fragment: residues 1-320. Synonym: protein-tyrosine phosphatase 1b,ptp-1b. Engineered: yes. Mutation: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: ptpn1, ptp1b. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

2.80Å

R-factor:

0.210

R-free:

0.268

Authors:

D.Barford,A.Salmeen,N.K.Tonks

Key ref:

A.Haque et al. (2011). Conformation-sensing antibodies stabilize the oxidized form of PTP1B and inhibit its phosphatase activity. Cell, 147, 185-198. PubMed id: 21962515

Date:

22-Jul-11

Release date:

31-Aug-11

PROCHECK

	Headers

	References

Protein chain

P18031 (PTN1_HUMAN) - Tyrosine-protein phosphatase non-receptor type 1 from Homo sapiens

Seq: Struc:					435 a.a. 281 a.a.*

Key:

PfamA domain

Secondary structure

CATH domain

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



		Enzyme reactions

Enzyme class:

E.C.3.1.3.48 - protein-tyrosine-phosphatase.

[IntEnz] [ExPASy] [KEGG] [BRENDA]

Reaction:

O-phospho-L-tyrosyl-[protein] + H2O = L-tyrosyl-[protein] + phosphate

O-phospho-L-tyrosyl-[protein]	+	H2O	=	L-tyrosyl-[protein]	+	phosphate

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

Key reference

	Cell 147:185-198 (2011)
PubMed id: 21962515

Conformation-sensing antibodies stabilize the oxidized form of PTP1B and inhibit its phosphatase activity.
A.Haque, J.N.Andersen, A.Salmeen, D.Barford, N.K.Tonks.

ABSTRACT

No abstract given.

Literature references that cite this PDB file's key reference

PubMed id

Reference

22743979

A.D.Lawson (2012).
Antibody-enabled small-molecule drug discovery.

Nat Rev Drug Discov, 11, 519-525.

The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time.