1IM0

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

Summary for 1IM0

Entry DOI	10.2210/pdb1im0/pdb
Related	1FW2 1FW3 1ILD 1ILZ 1QD5 1QD6
Descriptor	OUTER MEMBRANE PHSOPHOLIPASE A, octyl beta-D-glucopyranoside, (4S)-2-METHYL-2,4-PENTANEDIOL, ... (4 entities in total)
Functional Keywords	anti-parallel beta barrel, membrane phospholipase, membrane protein, serine hydrolase, catalytic triad, hydrolase
Biological source	Escherichia coli
Cellular location	Cell outer membrane; Multi-pass membrane protein: P0A921
Total number of polymer chains	1
Total formula weight	33017.85
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: 2023-09-20)
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 Cited by PubMed: 11567087 DOI: 10.1110/ps.17701 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.98 Å)

Structure validation