› 2cij

X-ray diffraction
2.4Å resolution

membrane-bound glutamate carboxypeptidase II (GCPII) with bound methionine

Released:
DOI: 10.2210/pdb2cij/pdb
PDB entry 2cij coloured by chain, front view.
PDB entry 2cij coloured by chain, side view.
PDB entry 2cij coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Glutamate Carboxypeptidase II
Mesters JR, Hilgenfeld R
Handbook of Metalloproteins 4 681- (2011)

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 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: 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:
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 MET 1 x MET
Ligand ZN 2 x ZN
Ligand CA 1 x CA
Ligand CL 1 x CL
Ligand NAG 3 x NAG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X13
Spacegroup: I222
Unit cell:
a: 102.692Å b: 130.777Å c: 160.303Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.174 0.172 0.219
Expression system: Drosophila melanogaster

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