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PDBe Entry: 1ilz 
OUTER MEMBRANE PHOSPHOLIPASE A FROM ESCHERICHIA COLI N156A ACTIVE SITE MUTANT pH 6.1
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HYDROLASE, MEMBRANE PROTEIN
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X-RAY DIFFRACTION
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Resolution: 2.5 Å, R-factor: 22.2%, Free R-factor: 26.8%, Spacegroup: P 31 2 1
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03/10/2001, deposition: 09/05/2001, last revision: 24/02/2009
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Snijder, H.J.; Van Eerde, J.H.; Kingma, R.L.; Kalk, K.H.; Dekker, N.; Egmond, M.R.; Dijkstra, B.W.
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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. vol:10, pag:1962-1969 (2001) [PubMed ID 11567087 ]
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ANTI-PARALLEL BETA BARREL, MEMBRANE PHOSPHOLIPASE, MEMBRANE PROTEIN, SERINE HYDROLASE, CATALYTIC TRIAD, ASN ALA MUTATION, HYDROLASE
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3.1.1.32 ExPASy BRENDA 3.1.1.4 ExPASy BRENDA (A)
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Escherichia coli 562(A)
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Phospholipase A1 precursor (EC 3.1.1.32) (EC 3.1.1.4) (Detergent-resistant phospholipase A) (DR-phospholipase A) (Phosphatidylcholine 1-acylhydrolase) (Outer membrane phospholipase A) (OM PLA) (OMPLA) P0A921 (A)
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A
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1qd5, 1qd6, 1fw2, 1ild, 1fw3, 1im0
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| A |
OUTER MEMBRANE PHOSPHOLIPASE A |
Protein |
P0A921 (PA1_ECOLI)
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275 |
93% |
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| A |
SUGAR (B-OCTYLGLUCOSIDE) |
BOG
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| A |
(4S)-2-METHYL-2,4-PENTANEDIOL |
MPD
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