PDBe 4ngm

X-ray diffraction
1.84Å resolution

Crystal Structure of Glutamate Carboxypeptidase II in a complex with urea-based inhibitor

Released:

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:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutamate carboxypeptidase 2 Chain: A
Molecule details ›
Chain: A
Length: 739 amino acids
Theoretical weight: 83.2 KDa
Source organism: Homo sapiens
Expression system: Drosophila melanogaster
UniProt:
  • Canonical: Q04609 (Residues: 44-750; Coverage: 94%)
  • Best match: Q04609-6 (Residues: 1-693)
Gene names: FOLH, FOLH1, GIG27, NAALAD1, PSM, PSMA
Sequence domains:
Structure domains:

Ligands and Environments


No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.2
Spacegroup: I222
Unit cell:
a: 101.3Å b: 130.193Å c: 158.789Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.171 0.17 0.206
Expression system: Drosophila melanogaster