1GBI

ALPHA-LYTIC PROTEASE WITH MET 190 REPLACED BY ALA AND GLY 216 REPLACED BY LEU COMPLEX WITH METHOXYSUCCINYL-ALA-ALA-PRO-PHENYLALANINE BORONIC ACID

Summary for 1GBI

Related PRD IDPRD_000315
DescriptorALPHA-LYTIC PROTEASE, METHOXYSUCCINYL-ALA-ALA-PRO-PHENYLALANINE BORONIC ACID INHIBITOR, SULFATE ION, ... (4 entities in total)
Functional Keywordsactive-site mutation, serine proteinase, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
Biological sourceLysobacter enzymogenes
Total number of polymer chains2
Total molecular weight20581.61
Authors
Mace, J.E.,Agard, D.A. (deposition date: 1995-09-06, release date: 1996-01-29, Last modification date: 2012-12-12)
Primary citation
Mace, J.E.,Agard, D.A.
Kinetic and structural characterization of mutations of glycine 216 in alpha-lytic protease: a new target for engineering substrate specificity.
J.Mol.Biol., 254:720-736, 1995
PubMed: 7500345 (PDB entries with the same primary citation)
DOI: 10.1006/jmbi.1995.0650
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (2.3 Å)
?

Structure validation

ClashscoreRamachandran outliersSidechain outliersRSRZ outliers50 3.5%0MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution
Download full validation reportDownload
171916
PDB entries from 2020-12-02