1GBL

ALPHA-LYTIC PROTEASE WITH MET 190 REPLACED BY ALA COMPLEX WITH METHOXYSUCCINYL-ALA-ALA-PRO-LEUCINE BORONIC ACID

Replaces:  4LPR

Summary for 1GBL

Related PRD IDPRD_000317
DescriptorALPHA-LYTIC PROTEASE, METHOXYSUCCINYL-ALA-ALA-PRO-LEUCINE 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 weight20395.43
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 (2.15 Å)
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Structure validation

ClashscoreRamachandran outliersSidechain outliersRSRZ outliers204.2%0MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution