5o5t

X-ray diffraction
1.43Å resolution

X-ray structure of human glutamate carboxypeptidase II (GCPII) in complex with a urea based inhibitor PSMA 1007

Released:
Source organism: Homo sapiens
Entry authors: Barinka C, Novakova Z, Motlova L

Function and Biology Details

Reaction catalysed:
Release of an unsubstituted, C-terminal glutamyl residue, typically from Ac-Asp-Glu or folylpoly-gamma-glutamates.

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-170042 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (4 distinct):
Glutamate carboxypeptidase 2 Chain: A
Molecule details ›
Chain: A
Length: 707 amino acids
Theoretical weight: 79.61 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:

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer : NEW Components: NAG, BMA
Carbohydrate polymer : NEW Components: NAG, BMA, MAN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PETRA III, EMBL c/o DESY BEAMLINE P13 (MX1)
Spacegroup: I222
Unit cell:
a: 101.657Å b: 130.159Å c: 159.16Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.139 0.138 0.173
Expression system: Drosophila melanogaster