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PDBsum entry 4p4e

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protein ligands metals links
Hydrolase PDB id
4p4e

 

 

 

 

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Contents
Protein chain
694 a.a.
Ligands
NAG-NAG
NAG-NAG-FUC ×2
NAG-NAG-BMA
NAG-NAG-BMA-MAN
NAG ×2
2G4
Metals
_ZN ×2
_CA
_CL
Waters ×562
PDB id:
4p4e
Name: Hydrolase
Title: X-ray structure of human glutamate carboxypeptidase ii (gcpii) in complex with a phosphoramidate inhibitor mp1d
Structure: Glutamate carboxypeptidase 2. Chain: a. Fragment: unp residues 44-750. Synonym: cell growth-inhibiting gene 27 protein,folate hydrolase 1, folylpoly-gamma-glutamate carboxypeptidase,fgcp,glutamate carboxypeptidase ii,gcpii,membrane glutamate carboxypeptidase,mgcp,n- acetylated-alpha-linked acidic dipeptidase i,naaladase i,prostate- specific membrane antigen,psma,pteroylpoly-gamma-glutamate carboxypeptidase.
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: folh1, folh, naalad1, psm, psma, gig27. Expressed in: drosophila melanogaster. Expression_system_taxid: 7227. Expression_system_cell_line: schneider's s2 cells.
Resolution:
1.67Å     R-factor:   0.154     R-free:   0.183
Authors: C.Barinka
Key ref: Z.Novakova et al. (2016). Design of composite inhibitors targeting glutamate carboxypeptidase II: the importance of effector functionalities. Febs J, 283, 130-143. PubMed id: 26460595 DOI: 10.1111/febs.13557
Date:
12-Mar-14     Release date:   20-May-15    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q04609  (FOLH1_HUMAN) -  Glutamate carboxypeptidase 2 from Homo sapiens
Seq:
Struc:
 
Seq:
Struc:
750 a.a.
694 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.3.4.17.21  - glutamate carboxypeptidase Ii.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Release of an unsubstituted, C-terminal glutamyl residue, typically from Ac-Asp-Glu or folylpoly-gamma-glutamates.
      Cofactor: Zn(2+)

 

 
DOI no: 10.1111/febs.13557 Febs J 283:130-143 (2016)
PubMed id: 26460595  
 
 
Design of composite inhibitors targeting glutamate carboxypeptidase II: the importance of effector functionalities.
Z.Novakova, J.Cerny, C.J.Choy, J.R.Nedrow, J.K.Choi, J.Lubkowski, C.E.Berkman, C.Barinka.
 
  ABSTRACT  
 
No abstract given.

 

 

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