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1IM0

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

Functional Information from GO Data
ChainGOidnamespacecontents
A0004620molecular_functionphospholipase activity
A0006629biological_processlipid metabolic process
A0016020cellular_componentmembrane
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues133
DetailsTransmembrane: {"description":"Beta stranded"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues66
DetailsTopological domain: {"description":"Extracellular"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues14
DetailsTopological domain: {"description":"Periplasmic"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"2040286","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues3
DetailsBinding site: {"description":"in dimeric form"}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsBinding site: {"description":"in monomeric form"}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1qd6
ChainResidueDetails
AHIS142
ASER144

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1qd6
ChainResidueDetails
AGLY146

site_idMCSA1
Number of Residues7
DetailsM-CSA 650
ChainResidueDetails
ASER106metal ligand
AHIS142proton acceptor, proton donor
ASER144covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor
AGLY146electrostatic stabiliser
AARG147metal ligand
ASER152metal ligand
AALA156electrostatic stabiliser, increase basicity

243911

PDB entries from 2025-10-29

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