Brand  (β version)

PDB ID: 4OC3

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Ligands
Code Name Style Show Link
2QP N~2~-{[(1s)-1-carboxy-2-(furan-2-yl)ethyl]carbamoyl}-N~6~-(4-iodobenzoyl)-L-lysine PoSSuM
CA Calcium ion PoSSuM
CL Chloride ion PoSSuM
ZN Zinc ion PoSSuM
Non-standard Residues
Code Name Show
Glycosylation
Code Name Emphasize
BMA Beta-D-mannopyranose
FUC Alpha-L-fucopyranose
MAN Alpha-D-mannopyranose
NAG 2-acetamido-2-deoxy-beta-D-glucopyranose
Modification
Code Name Show

Structure summary

Code : 4OC3   PDBj   RCSB PDB   PDBe
Header : hydrolase/hydrolase inhibitor
Title : X-ray structure of of human glutamate carboxypeptidase II (GCPII) in a complex with CFIBzL, a urea-based inhibitor N~2~-{[(1S)-1-carboxy-2-(furan-2-yl)ethyl]carbamoyl}-N~6~-(4-iodobenzoyl)-L-lysine
Release Data : 2014-05-21
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
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_strain: Schneider's S2 cells
expression_system_vector_type: plasmid
Authors : Pavlicek, J., Ptacek, J., Cerny, J., Byun, Y., Skultetyova, L., Pomper, M., Lubkowski, J., Barinka, C.
Keywords : hydrolase, metallopeptidase, hydrolase-hydrolase inhibitor complex
Exp. method : X-RAY DIFFRACTION ( 1.79 Å )
Citation :

Structural characterization of P1'-diversified urea-based inhibitors of glutamate carboxypeptidase II.

Pavlicek, J.,Ptacek, J.,Cerny, J.  et al.
(2014)  Bioorg.Med.Chem.Lett.  24 : 2340 - 2345

PubMed: 24731280
DOI: 10.1016/j.bmcl.2014.03.066

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 -
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