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PDBsum entry 3pxj

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

 

 

 

 

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Contents
Protein chains
199 a.a.
187 a.a.
Waters ×138
PDB id:
3pxj
Name: Hydrolase
Title: Tandem ig repeats of dlar
Structure: Tyrosine-protein phosphatase lar. Chain: a, b, c, d. Fragment: ig domains 1 and 2 (unp residues 32-237). Synonym: protein-tyrosine-phosphate phosphohydrolase, dlar. Engineered: yes
Source: Drosophila melanogaster. Fruit fly. Organism_taxid: 7227. Gene: lar, cg10443. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Resolution:
2.30Å     R-factor:   0.225     R-free:   0.261
Authors: B.H.Biersmith,S.Bouyain
Key ref: B.H.Biersmith et al. (2011). The immunoglobulin-like domains 1 and 2 of the protein tyrosine phosphatase LAR adopt an unusual horseshoe-like conformation. J Mol Biol, 408, 616-627. PubMed id: 21402080
Date:
10-Dec-10     Release date:   23-Mar-11    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P16621  (LAR_DROME) -  Tyrosine-protein phosphatase Lar from Drosophila melanogaster
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
2029 a.a.
199 a.a.
Protein chains
Pfam   ArchSchema ?
P16621  (LAR_DROME) -  Tyrosine-protein phosphatase Lar from Drosophila melanogaster
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
2029 a.a.
187 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: Chains A, B, C, D: 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    
 
 
J Mol Biol 408:616-627 (2011)
PubMed id: 21402080  
 
 
The immunoglobulin-like domains 1 and 2 of the protein tyrosine phosphatase LAR adopt an unusual horseshoe-like conformation.
B.H.Biersmith, M.Hammel, E.R.Geisbrecht, S.Bouyain.
 
  ABSTRACT  
 
No abstract given.

 

 

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