1IM0

OUTER MEMBRANE PHOSPHOLIPASE A FROM ESCHERICHIA COLI N156A ACTIVE SITE MUTANT PH 8.3

Summary for 1IM0
Related1FW2 1FW3 1ILD 1ILZ 1QD5 1QD6
DescriptorOUTER MEMBRANE PHSOPHOLIPASE A, octyl beta-D-glucopyranoside, (4S)-2-METHYL-2,4-PENTANEDIOL, ... (4 entities in total)
Functional Keywordsanti-parallel beta barrel, membrane phospholipase, membrane protein, serine hydrolase, catalytic triad, hydrolase
Biological sourceEscherichia coli
Cellular locationCell outer membrane; Multi-pass membrane protein: P0A921
Total number of polymer chains1
Total formula weight33017.85
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: 2020-07-29)
Primary citationDekker, N.,Dijkstra, B.W.,Egmond, M.R.,Kalk, K.H.,Kingma, R.L.,Snijder, H.J.,Van Eerde, J.H.
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
DOI: 110.1110/ps.17701
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.98 Å)
Structure validation
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PDB entries from 2021-06-16