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PDBsum entry 3brh

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protein ligands Protein-protein interface(s) links
Hydrolase PDB id
3brh

 

 

 

 

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Contents
Protein chains
296 a.a. *
Ligands
ASP-ASN-GLU-TYR-
THR-ALA-ARG
ASP-ASN-GLU-TYR
PO4 ×2
Waters ×295
* Residue conservation analysis
PDB id:
3brh
Name: Hydrolase
Title: Protein tyrosine phosphatase ptpn-22 (lyp) bound to the mono- phosphorylated lck active site peptide
Structure: Tyrosine-protein phosphatase non-receptor type 22. Chain: a, b. Fragment: substrate trapped catalytic domain. Synonym: hematopoietic cell protein-tyrosine phosphatase 70z-pep, lymphoid phosphatase,lyp,pest-domain phosphatase,pep. Engineered: yes. Mutation: yes. Lck active site peptide. Chain: c, d.
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: ptpn22, ptpn8. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Other_details: the peptide was chemically synthesized. The sequence of the peptide is naturally found in home sapiens(human).
Resolution:
2.20Å     R-factor:   0.191     R-free:   0.264
Authors: R.D.Seidel,J.Love,A.Piserchio,D.Cowburn
Key ref: R.Seidel et al. Lyp/ptpn22 phosphatase domain: substrate recognition and specificity for src family kinases. To be published, .
Date:
21-Dec-07     Release date:   17-Feb-09    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q9Y2R2  (PTN22_HUMAN) -  Tyrosine-protein phosphatase non-receptor type 22 from Homo sapiens
Seq:
Struc:
 
Seq:
Struc:
807 a.a.
296 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
Bound ligand (Het Group name = PO4)
corresponds exactly
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

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