Brand  (β version)

PDB ID: 4MCQ

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Ligands
Code Name Style Show Link
29C N-(4-{[(2-amino-4-oxo-3,4-dihydropteridin-6-yl)methyl]amino}benzoyl)-L-gamma-glutamyl-L-gamma-glutamyl-L-glutamic acid PoSSuM
CA Calcium ion PoSSuM
CL Chloride ion 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
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Structure summary

Code : 4MCQ   PDBj   RCSB PDB   PDBe
Header : HYDROLASE
Title : A high resolution structure of human glutamate carboxypeptidase II (GCPII) in complex with folyldi-gamma-L-glutamic acid (pteroyltri-gamma-L-glutamic acid)
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: Glutamate carboxypeptidase II, unp residues 44-750
mutation: E424A
Source :
mol_id organism_scientific organism_common expression_system
1 Homo sapiens  (taxid:9606) Human Drosophila Melanogaster  (taxid:7227)
gene: FOLH1, FOLH, NAALAD1, PSM, PSMA, GIG27
expression_system_cell_line: Schneider's S2
Authors : Navratil, M., Barinka, C.
Keywords : hydrolase, metallopeptidase, hydrolase-hydrolase inhibitor complex, Prostate specific membrane antigen, folate hydrolase 1, FOLH1
Exp. method : X-RAY DIFFRACTION ( 2.00 Å )
Citation :

Structural and biochemical characterization of the folyl-poly-gamma-l-glutamate hydrolyzing activity of human glutamate carboxypeptidase II.

Navratil, M.,Ptacek, J.,Sacha, P.  et al.
(2014)  Febs J.  281 : 3228 - 3242

PubMed: 24863754
DOI: 10.1111/febs.12857

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.