1H2Y

PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, Y473F MUTANT WITH COVALENTLY BOUND INHIBITOR Z-PRO-PROLINAL

Summary for 1H2Y

Related1E5T 1E8M 1E8N 1H2W 1H2X 1H2Z 1O6F 1O6G 1QFM 1QFS
Related PRD IDPRD_000692
DescriptorPROLYL ENDOPEPTIDASE, N-BENZYLOXYCARBONYL-L-PROLYL-L-PROLINAL, GLYCEROL, ... (4 entities in total)
Functional Keywordshydrolase, prolyl oligopeptidase, amnesia, alpha/ beta- hydrolase, beta-propeller, serine protease
Biological sourceSUS SCROFA (PIG)
Cellular locationCytoplasm P23687
Total number of polymer chains1
Total molecular weight81639.19
Authors
Rea, D.,Fulop, V. (deposition date: 2002-08-20, release date: 2002-11-11, Last modification date: 2013-03-06)
Primary citation
Szeltner, Z.,Rea, D.,Renner, V.,Fulop, V.,Polgar, L.
Electrostatic Effects and Binding Determinants in the Catalysis of Prolyl Oligopeptidase: Site Specific Mutagenesis at the Oxyanion Binding Site
J.Biol.Chem., 277:42613-, 2002
PubMed: 12202494 (PDB entries with the same primary citation)
DOI: 10.1074/JBC.M208043200
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (1.78 Å)
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Structure validation

ClashscoreRamachandran outliersSidechain outliers2 0.3% 1.0%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution
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PDB entries from 2020-09-23