› 3sjf

X-ray diffraction
1.65Å resolution

X-ray structure of human glutamate carboxypeptidase II in complex with a urea-based inhibitor (A25)

Released:
DOI: 10.2210/pdb3sjf/pdb
PDB entry 3sjf coloured by chain, front view.
PDB entry 3sjf coloured by chain, side view.
PDB entry 3sjf coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Novel substrate-based inhibitors of human glutamate carboxypeptidase II with enhanced lipophilicity.
Plechanovová A, Byun Y, Alquicer G, Skultétyová L, Mlčochová P, Němcová A, Kim HJ, Navrátil M, Mease R, Lubkowski J, Pomper M, Konvalinka J, Rulíšek L, Bařinka C
J Med Chem 54 7535-46 (2011)
PMID: 21923190

Function and Biology Details

Reaction catalysed: 
Release of an unsubstituted, C-terminal glutamyl residue, typically from Ac-Asp-Glu or folylpoly-gamma-glutamates.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-170042 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (3 distinct):
Glutamate carboxypeptidase 2 Chain: A
Molecule details ›
Chain: A
Length: 709 amino acids
Theoretical weight: 79.86 KDa
Source organism: Homo sapiens
Expression system: Drosophila melanogaster
UniProt:
  • Canonical: Q04609 (Residues: 44-750; Coverage: 94%)
Gene names: FOLH, FOLH1, GIG27, NAALAD1, PSM, PSMA
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG, BMA, MAN
Carbohydrate polymer
5 bound ligands:
Ligand NAG 3 x NAG
Ligand ZN 2 x ZN
Ligand CA 1 x CA
Ligand CL 1 x CL
Ligand JRG 1 x JRG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: I222
Unit cell:
a: 101.545Å b: 130.431Å c: 159.156Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.159 0.159 0.178
Expression system: Drosophila melanogaster

Quick links

Citations

2 review citations

Blockade of N-acetylaspartylglutamate peptidases: a novel protective strategy for brain injuries and neurological disorders.
Zhong et al. (2014)
1 more

1 mention without citation

Novel substrate-based inhibitors of human glutamate carboxypeptidase II with enhanced lipophilicity.
Plechanovová et al. (2011)