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1QD5

OUTER MEMBRANE PHOSPHOLIPASE A FROM ESCHERICHIA COLI

Functional Information from GO Data
ChainGOidnamespacecontents
A0004620molecular_functionphospholipase activity
A0004622molecular_functionphosphatidylcholine lysophospholipase activity
A0004623molecular_functionphospholipase A2 activity
A0005509molecular_functioncalcium ion binding
A0006629biological_processlipid metabolic process
A0008970molecular_functionphospholipase A1 activity
A0009279cellular_componentcell outer membrane
A0016020cellular_componentmembrane
A0016042biological_processlipid catabolic process
A0016787molecular_functionhydrolase activity
A0042803molecular_functionprotein homodimerization activity
A0046471biological_processphosphatidylglycerol metabolic process
A0046872molecular_functionmetal ion binding
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_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
AASN156electrostatic stabiliser, increase basicity

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

246905

PDB entries from 2025-12-31

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