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PDBsum entry 4grz

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protein ligands links
Hydrolase PDB id
4grz
Jmol
Contents
Protein chain
282 a.a.
Ligands
PO4
Waters ×391
PDB id:
4grz
Name: Hydrolase
Title: Crystal structure of shp1 catalytic domain with po4
Structure: Tyrosine-protein phosphatase non-receptor type 6. Chain: a. Fragment: phosphatase domain unp residues 242-528. Synonym: hematopoietic cell protein-tyrosine phosphatase, p tyrosine phosphatase 1c, ptp-1c, protein-tyrosine phosphata sh-ptp1. Engineered: yes. Mutation: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: hcp, ptp1c, ptpn6, shp-1. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Resolution:
1.37Å     R-factor:   0.170     R-free:   0.189
Authors: N.L.Alicea-Velazquez,J.Jakoncic,T.J.Boggon
Key ref: N.L.Alicea-Velázquez et al. (2013). Structure-guided studies of the SHP-1/JAK1 interaction provide new insights into phosphatase catalytic domain substrate recognition. J Struct Biol, 181, 243-251. PubMed id: 23296072 DOI: 10.1016/j.jsb.2012.12.009
Date:
27-Aug-12     Release date:   19-Dec-12    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P29350  (PTN6_HUMAN) -  Tyrosine-protein phosphatase non-receptor type 6
Seq:
Struc:
 
Seq:
Struc:
595 a.a.
282 a.a.*
Key:    PfamA 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
Bound ligand (Het Group name = PO4)
corresponds exactly
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.jsb.2012.12.009 J Struct Biol 181:243-251 (2013)
PubMed id: 23296072  
 
 
Structure-guided studies of the SHP-1/JAK1 interaction provide new insights into phosphatase catalytic domain substrate recognition.
N.L.Alicea-Velázquez, J.Jakoncic, T.J.Boggon.
 
  ABSTRACT  
 
No abstract given.