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Structure paper

TitleStructural insight into the evolutionary and pharmacologic homology of glutamate carboxypeptidases II and III
Journal, issue, pagesFebs J., Vol. 276, Page 4448-4462, Year 2009
Publish dateNov 28, 2008 (structure data deposition date)
AuthorsHlouchova, K. / Barinka, C. / Konvalinka, J. / Lubkowski, J.
External linksFebs J. / PubMed:19678840
MethodsX-ray diffraction
Resolution1.29 - 1.56 Å
Structure data

PDB-3fec:
Crystal structure of human Glutamate Carboxypeptidase III (GCPIII/NAALADase II), pseudo-unliganded
Method: X-RAY DIFFRACTION / Resolution: 1.49 Å

PDB-3fed:
The high resolution structure of human glutamate carboxypeptidase III (GCPIII/NAALADase II) in complex with a transition state analog of Glu-Glu
Method: X-RAY DIFFRACTION / Resolution: 1.29 Å

PDB-3fee:
The high resolution structure of human glutamate carboxypeptidase III (GCPIII/NAALADase II) in complex with quisqualic acid
Method: X-RAY DIFFRACTION / Resolution: 1.56 Å

PDB-3ff3:
The high resolution structure of human glutamate carboxypeptidase III (GCPIII/NAALADase II) in complex with L-glutamate
Method: X-RAY DIFFRACTION / Resolution: 1.37 Å

Chemicals

ChemComp-GLU:
GLUTAMIC ACID

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

ChemComp-ZN:
Unknown entry

ChemComp-CL:
Unknown entry

ChemComp-CA:
Unknown entry

ChemComp-GOL:
GLYCEROL

ChemComp-MPO:
3[N-MORPHOLINO]PROPANE SULFONIC ACID / pH buffer*YM

ChemComp-HOH:
WATER

ChemComp-BIX:
(2S)-2-{[(S)-[(3S)-3-amino-3-carboxypropyl](hydroxy)phosphoryl]methyl}pentanedioic acid

ChemComp-QUS:
(S)-2-AMINO-3-(3,5-DIOXO-[1,2,4]OXADIAZOLIDIN-2-YL)-PROPIONIC ACID / agonist*YM

Source
  • homo sapiens (human)
KeywordsHYDROLASE / metallopeptidase; bimetallic active site; N-glycosylation; calcium cation; chloride anion; zinc ions; / Carboxypeptidase / Dipeptidase / Glycoprotein / Membrane / Metal-binding / Metalloprotease / Multifunctional enzyme / Protease / Signal-anchor / Transmembrane / metallopeptidase / bimetallic active site / N-glycosylation / calcium cation / chloride anion / zinc ions / metallopeptidase; bimetallic active site; N-glycosylation; calcium cation; chloride anion; zinc ions

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