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PDBsum entry 2pi7

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protein ligands Protein-protein interface(s) links
Hydrolase PDB id
2pi7

 

 

 

 

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JSmol PyMol  
Contents
Protein chains
294 a.a. *
Ligands
NO3 ×2
Waters ×182
* Residue conservation analysis
PDB id:
2pi7
Name: Hydrolase
Title: Structure of the catalytic domain of the chick retinal neurite inhibitor-receptor protein tyrosine phosphatase cryp-2/cptpro
Structure: Protein tyrosine phosphatase cryp-2. Chain: a, b. Fragment: catalytic domain, residues 956-1267. Engineered: yes
Source: Gallus gallus. Chicken. Organism_taxid: 9031. Gene: cryp2. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.59Å     R-factor:   0.227     R-free:   0.287
Authors: T.S.Girish,B.Gopal
Key ref:
T.S.Girish and B.Gopal (2007). The crystal structure of the catalytic domain of the chick retinal neurite inhibitor-receptor protein tyrosine phosphatase CRYP-2/cPTPRO. Proteins, 68, 1011-1015. PubMed id: 17546659 DOI: 10.1002/prot.21424
Date:
13-Apr-07     Release date:   01-May-07    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q98945  (Q98945_CHICK) -  protein-tyrosine-phosphatase from Gallus gallus
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1267 a.a.
294 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 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
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    Key reference    
 
 
DOI no: 10.1002/prot.21424 Proteins 68:1011-1015 (2007)
PubMed id: 17546659  
 
 
The crystal structure of the catalytic domain of the chick retinal neurite inhibitor-receptor protein tyrosine phosphatase CRYP-2/cPTPRO.
T.S.Girish, B.Gopal.
 
  ABSTRACT  
 
No abstract given.

 
  Selected figure(s)  
 
Figure 1.
Figure 1. (a) Sequence alignment of PTP D1 domains of CRYP-2, RPTP- and RPTP- , and PTP1B. The secondary structure elements corresponding to CRYP-2 are shown. A grey background has been used to highlight residues involved in oligomerization. These are poorly conserved. (b) The quaternary arrangement of CRYP-2 showing the location of the two active sites. The active site of CRYP-2 (highlighted by the red circle) is not occluded by oligomerization. The active site cysteine, aspartate, proline, tryptophan, and the bound nitrate ion are depicted in ball and stick representation. (c) Both open and closed conformations of the active site lid are seen in the crystal structure. In this superposition, the red ribbon representation is for CRYP-2 while the superposed PTP1B conformation is seen in grey. (d and e) The active site of CRYP-2 contains a nitrate ion in both the closed and open conformations. Panels d (closed conformation) and e (open conformation) show the (2Fo-Fc) electron density map calculated at 1.2 for the residues that surround the active site as well as the bound nitrate ion.
 
  The above figure is reprinted by permission from John Wiley & Sons, Inc.: Proteins (2007, 68, 1011-1015) copyright 2007.  

 

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