1QD6

OUTER MEMBRANE PHOSPHOLIPASE A FROM ESCHERICHIA COLI

Summary for 1QD6

Related1QD5
DescriptorOUTER MEMBRANE PHOSPHOLIPASE (OMPLA), PROTEIN (OUTER MEMBRANE PHOSPHOLIPASE (OMPLA)), CALCIUM ION, ... (5 entities in total)
Functional Keywordsanti-parallel beta barrel dimer, membrane protein
Biological sourceEscherichia coli
Cellular locationCell outer membrane ; Multi-pass membrane protein  P0A921 P0A921
Total number of polymer chains4
Total molecular weight58925.64
Authors
Snijder, H.J.,Ubarretxena-Belandia, I.,Blaauw, M.,Kalk, K.H.,Verheij, H.M.,Egmond, M.R.,Dekker, N.,Dijkstra, B.W. (deposition date: 1999-07-09, release date: 1999-10-25, Last modification date: 2018-01-31)
Primary citation
Snijder, H.J.,Ubarretxena-Belandia, I.,Blaauw, M.,Kalk, K.H.,Verheij, H.M.,Egmond, M.R.,Dekker, N.,Dijkstra, B.W.
Structural evidence for dimerization-regulated activation of an integral membrane phospholipase.
Nature, 401:717-721, 1999
PubMed: 10537112 (PDB entries with the same primary citation)
DOI: 10.1038/44890
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (2.1 Å)
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Structure validation

ClashscoreRamachandran outliersSidechain outliers70.4%7.0%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution
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