Brand  (β version)

PDB ID: 4NGR

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Ligands
Code Name Style Show Link
CA Calcium ion PoSSuM
CL Chloride ion PoSSuM
J21 N-{[(1s)-5-({2-[2-(acetylamino)ethoxy]-4-bromobenzoyl}amino)-1-carboxypentyl]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 : 4NGR   PDBj   RCSB PDB   PDBe
Header : HYDROLASE/HYDROLASE INHIBITOR
Title : Crystal Structure of Glutamate Carboxypeptidase II in a complex with urea-based inhibitor
Release Data : 2014-06-18
Compound :
mol_id molecule chains synonym
1 Glutamate carboxypeptidase 2 A Cell growth-inhibiting gene 27 protein, Folate hydrolase 1, Folylpoly-gamma-glutamate carboxypeptidase, FGCP, Glutamate carboxypeptidase II, GCPII, Membrane glutamate carboxypeptidase, mGCP, N-acetylated-alpha-linked acidic dipeptidase I, NAALADase I, Prostate-specific membrane antigen, PSM, PSMA, Pteroylpoly-gamma-glutamate carboxypeptidase
ec: 3.4.17.21
fragment: Extracellular domain, UNP residues 44-750
Source :
mol_id organism_scientific organism_common expression_system
1 Homo sapiens  (taxid:9606) Human Drosophila melanogaster  (taxid:7227)
gene: FOLH, FOLH1, GIG27, NAALAD1, PSM, PSMA
expression_system_cell_line: SCHNEIDER 2(S2) CELLS
expression_system_vector_type: BACULOVIRUS
expression_system_plasmid: pMT/Bip
Authors : Tykvart, J., Pachl, P.
Keywords : hydrolase, glutamate carboxypeptidase II, PSMA, NAALADASE, urea-based inhibitor, caboxypeptidase, glycoprotein, metallopeptidase, HYDROLASE-HYDROLASE INHIBITOR complex
Exp. method : X-RAY DIFFRACTION ( 1.9000 Å )
Citation :

Rational design of urea-based glutamate carboxypeptidase II (GCPII) inhibitors as versatile tools for specific drug targeting and delivery.

Tykvart, J.,Schimer, J.,Barinkova, J.  et al.
(2014)  Bioorg.Med.Chem.  22 : 4099 - 4108

PubMed: 24954515
DOI: 10.1016/j.bmc.2014.05.061

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.