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PDBsum entry 3rau

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protein ligands Protein-protein interface(s) links
Hydrolase PDB id
3rau
Jmol
Contents
Protein chain
358 a.a.
Ligands
ACT ×8
EDO ×2
GOL
Waters ×299
PDB id:
3rau
Name: Hydrolase
Title: Crystal structure of the hd-ptp bro1 domain
Structure: Tyrosine-protein phosphatase non-receptor type 23 chain: a, b. Fragment: unp residues 2-361. Synonym: his domain-containing protein tyrosine phosphatase protein tyrosine phosphatase td14, ptp-td14. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: ptpn23, kiaa1471. Expressed in: escherichia coli. Expression_system_taxid: 562
Resolution:
1.95Å     R-factor:   0.174     R-free:   0.215
Authors: R.L.Mu,J.S.Jiang,G.Snyder,P.Smith,T.Xiao
Key ref: P.Sette et al. (2011). The Phe105 loop of Alix Bro1 domain plays a key role in HIV-1 release. Structure, 19, 1485-1495. PubMed id: 21889351 DOI: 10.1016/j.str.2011.07.016
Date:
28-Mar-11     Release date:   14-Sep-11    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q9H3S7  (PTN23_HUMAN) -  Tyrosine-protein phosphatase non-receptor type 23
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1636 a.a.
358 a.a.
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.3.1.3.48  - Protein-tyrosine-phosphatase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Protein tyrosine phosphate + H2O = protein tyrosine + phosphate
Protein tyrosine phosphate
+ H(2)O
= protein tyrosine
+ phosphate
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     regulation of cell migration   3 terms 
  Biochemical function     protein tyrosine phosphatase activity     1 term  

 

 
    reference    
 
 
DOI no: 10.1016/j.str.2011.07.016 Structure 19:1485-1495 (2011)
PubMed id: 21889351  
 
 
The Phe105 loop of Alix Bro1 domain plays a key role in HIV-1 release.
P.Sette, R.Mu, V.Dussupt, J.Jiang, G.Snyder, P.Smith, T.S.Xiao, F.Bouamr.
 
  ABSTRACT  
 
No abstract given.