8bo8

X-ray diffraction
1.55Å resolution

X-ray structure of human glutamate carboxypeptidase II (GCPII) in complex with an inhibitor P17

Released:
Source organism: Homo sapiens
Entry authors: Motlova L, Barinka C, Benesova M

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

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.2
Spacegroup: I222
Unit cell:
a: 101.887Å b: 130.286Å c: 159.702Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.203 0.202 0.226
Expression system: Drosophila melanogaster