1ILZ

OUTER MEMBRANE PHOSPHOLIPASE A FROM ESCHERICHIA COLI N156A ACTIVE SITE MUTANT pH 6.1

Summary for 1ILZ

Related1QD5 1QD6 1FW2 1ILD 1FW3 1IM0
DescriptorOUTER MEMBRANE PHOSPHOLIPASE A, B-OCTYLGLUCOSIDE, (4S)-2-METHYL-2,4-PENTANEDIOL, ... (4 entities in total)
Functional Keywordsanti-parallel beta barrel, membrane phospholipase, membrane protein, serine hydrolase, catalytic triad, asn ala mutation, hydrolase
Biological sourceEscherichia coli
Cellular locationCell outer membrane; Multi-pass membrane protein P0A921
Total number of polymer chains1
Total molecular weight33192.05
Authors
Snijder, H.J.,Van Eerde, J.H.,Kingma, R.L.,Kalk, K.H.,Dekker, N.,Egmond, M.R.,Dijkstra, B.W. (deposition date: 2001-05-09, release date: 2001-10-03, Last modification date: 2011-07-13)
Primary citation
Snijder, H.J.,Van Eerde, J.H.,Kingma, R.L.,Kalk, K.H.,Dekker, N.,Egmond, M.R.,Dijkstra, B.W.
Structural investigations of the active-site mutant Asn156Ala of outer membrane phospholipase A: function of the Asn-His interaction in the catalytic triad.
Protein Sci., 10:1962-1969, 2001
PubMed: 11567087 (PDB entries with the same primary citation)
DOI: 10.1110/ps.17701
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (2.5 Å)
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Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers0.276130.4%4.5%4.7%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution
Download full validation reportDownload