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1FW3

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
B0004620molecular_functionphospholipase activity
B0004622molecular_functionphosphatidylcholine lysophospholipase activity
B0004623molecular_functionphospholipase A2 activity
B0005509molecular_functioncalcium ion binding
B0006629biological_processlipid metabolic process
B0008970molecular_functionphospholipase A1 activity
B0009279cellular_componentcell outer membrane
B0016020cellular_componentmembrane
B0016042biological_processlipid catabolic process
B0016787molecular_functionhydrolase activity
B0042803molecular_functionprotein homodimerization activity
B0046471biological_processphosphatidylglycerol metabolic process
B0046872molecular_functionmetal ion binding
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues244
DetailsTransmembrane: {"description":"Beta stranded"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues132
DetailsTopological domain: {"description":"Extracellular"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues24
DetailsTopological domain: {"description":"Periplasmic"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"2040286","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues6
DetailsBinding site: {"description":"in dimeric form"}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsBinding site: {"description":"in monomeric form"}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1qd6
ChainResidueDetails
AHIS142
AS1H144
AGLY146

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1qd6
ChainResidueDetails
BHIS142
BS1H144
BGLY146

site_idMCSA1
Number of Residues7
DetailsM-CSA 650
ChainResidueDetails
ASER106metal ligand
AHIS142proton acceptor, proton donor
AS1H144covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor
APRO150electrostatic stabiliser
ATHR151metal ligand
AASN156metal ligand
ATHR160electrostatic stabiliser, increase basicity

site_idMCSA2
Number of Residues7
DetailsM-CSA 650
ChainResidueDetails
BSER106metal ligand
BHIS142proton acceptor, proton donor
BS1H144covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor
BPRO150electrostatic stabiliser
BTHR151metal ligand
BASN156metal ligand
BTHR160electrostatic stabiliser, increase basicity

246905

PDB entries from 2025-12-31

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