3bxm

X-ray diffraction
1.71Å resolution

Structure of an inactive mutant of human glutamate carboxypeptidase II [GCPII(E424A)] in complex with N-acetyl-Asp-Glu (NAAG)

Released:

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:
hetero tetramer (preferred)
PDBe Complex ID:
PDB-CPX-163446 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (4 distinct):
Glutamate carboxypeptidase 2 Chain: A
Molecule details ›
Chain: A
Length: 709 amino acids
Theoretical weight: 79.8 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:
N-Acetyl-Aspartyl-Glutamate (NAAG) Chain: I
Molecule details ›
Chain: I
Length: 3 amino acids
Theoretical weight: 288 Da
Source organism: Homo sapiens
Expression system: Not provided

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-BM
Spacegroup: I222
Unit cell:
a: 102.063Å b: 129.801Å c: 159.589Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.185 0.184 0.213
Expression systems:
  • Drosophila melanogaster
  • Not provided