Brand  (β version)

PDB ID: 3D7D

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Ligands
Code Name Style Show Link
CA Calcium ion PoSSuM
CL Chloride ion PoSSuM
FBD N-({(1r)-1-carboxy-2-[(4-fluorobenzyl)sulfanyl]ethyl}carbamoyl)-L-glutamic acid PoSSuM
ZN Zinc ion PoSSuM
Non-standard Residues
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Glycosylation
Code Name Emphasize
BMA Beta-D-mannopyranose
MAN Alpha-D-mannopyranose
NAG 2-acetamido-2-deoxy-beta-D-glucopyranose
Modification
Code Name Show

Structure summary

Code : 3D7D   PDBj   RCSB PDB   PDBe
Header : HYDROLASE
Title : A high resolution crystal structure of human glutamate carboxypeptidase II (GCPII) in a complex with DCFBD, a urea-based inhibitor
Release Data : 2008-12-30
Compound :
mol_id molecule chains synonym
1 Glutamate carboxypeptidase 2 A Glutamate carboxypeptidase II, Membrane glutamate carboxypeptidase, mGCP, N-acetylated-alpha-linked acidic dipeptidase I, NAALADase I, Pteroylpoly-gamma-glutamate carboxypeptidase, Folylpoly-gamma-glutamate carboxypeptidase, FGCP, Folate hydrolase 1, Prostate-specific membrane antigen, PSMA, PSM
ec: 3.4.17.21
Source :
mol_id organism_scientific organism_common expression_system
1 Homo sapiens  (taxid:9606) Human Drosophila melanogaster
gene: FOLH1, FOLH, NAALAD1, PSM, PSMA
expression_system_cell_line: Schneider's S2 cells
expression_system_vector_type: plasmid
Authors : Lubkowski, J., Barinka, C.
Keywords : prostate specific membrane antigen; metallopeptidase; folate hydrolase; glutamate carboxypeptidase II; Naaladase; DCFBD, urea-based inhibitor, Carboxypeptidase, Dipeptidase, Glycoprotein, Hydrolase, Membrane, Metal-binding, Metalloprotease, Multifunctional enzyme, Protease, Signal-anchor, Transmembrane
Exp. method : X-RAY DIFFRACTION ( 1.69 Å )
Citation :

Interactions between Human Glutamate Carboxypeptidase II and Urea-Based Inhibitors: Structural Characterization

Barinka, C.,Byun, Y.,Dusich, C.L.  et al.
(2008)  J.Med.Chem.  51 : 7737 - 7743

PubMed: 19053759
DOI: 10.1021/jm800765e

Reaction

Chain : A
UniProt : Q04609 (FOLH1_HUMAN)
Reaction: EC: Evidence:
Physiological Direction:
Release of an unsubstituted, C-terminal glutamyl residue, typically from Ac-Asp-Glu or folylpoly-gamma-glutamates. 3.4.17.21 -
-
Cofactor: Evidence: Note:
Zn(2+) ECO:0000269 | PubMed:16467855
ECO:0000269 | PubMed:17372356
ECO:0000269 | PubMed:17567119
ECO:0000269 | PubMed:18234225
ECO:0000269 | PubMed:19053759
ECO:0000269 | PubMed:19301871
Binds 2 Zn(2+) ions per subunit. Required for NAALADase activity.