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PDBsum entry 3qkp

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protein ligands links
Hydrolase PDB id
3qkp
Jmol
Contents
Protein chain
291 a.a.
Ligands
TRS
GOL ×2
Waters ×239
PDB id:
3qkp
Name: Hydrolase
Title: Protein tyrosine phosphatase 1b - apo w179f mutant with open
Structure: Tyrosine-protein phosphatase non-receptor type 1. Chain: a. Fragment: catalytic domain, residues 1-321. Synonym: protein-tyrosine phosphatase 1b, ptp-1b. Engineered: yes. Mutation: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: ptp1b, ptpn1. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Resolution:
2.05Å     R-factor:   0.206     R-free:   0.245
Authors: T.A.S.Brandao,S.J.Johnson,A.C.Hengge
Key ref: T.A.Brandão et al. (2012). The molecular details of WPD-loop movement differ in the protein-tyrosine phosphatases YopH and PTP1B. Arch Biochem Biophys, 525, 53-59. PubMed id: 22698963 DOI: 10.1016/j.abb.2012.06.002
Date:
01-Feb-11     Release date:   08-Aug-12    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P18031  (PTN1_HUMAN) -  Tyrosine-protein phosphatase non-receptor type 1
Seq:
Struc:
435 a.a.
291 a.a.*
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 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     dephosphorylation   2 terms 
  Biochemical function     phosphatase activity     2 terms  

 

 
    reference    
 
 
DOI no: 10.1016/j.abb.2012.06.002 Arch Biochem Biophys 525:53-59 (2012)
PubMed id: 22698963  
 
 
The molecular details of WPD-loop movement differ in the protein-tyrosine phosphatases YopH and PTP1B.
T.A.Brandão, S.J.Johnson, A.C.Hengge.
 
  ABSTRACT  
 
No abstract given.