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4X94

Crystal structure of Lysosomal Phospholipase A2 crystallized in the presence of methyl arachidonyl fluorophosphonate (hexagonal form)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004622molecular_functionphosphatidylcholine lysophospholipase activity
A0004623molecular_functionphospholipase A2 activity
A0005515molecular_functionprotein binding
A0005543molecular_functionphospholipid binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005654cellular_componentnucleoplasm
A0005764cellular_componentlysosome
A0006629biological_processlipid metabolic process
A0006631biological_processfatty acid metabolic process
A0006644biological_processphospholipid metabolic process
A0006650biological_processglycerophospholipid metabolic process
A0006651biological_processdiacylglycerol biosynthetic process
A0006658biological_processphosphatidylserine metabolic process
A0006672biological_processceramide metabolic process
A0008270molecular_functionzinc ion binding
A0008374molecular_functionO-acyltransferase activity
A0008970molecular_functionphospholipase A1 activity
A0009062biological_processfatty acid catabolic process
A0016020cellular_componentmembrane
A0016042biological_processlipid catabolic process
A0016411molecular_functionacylglycerol O-acyltransferase activity
A0016740molecular_functiontransferase activity
A0016746molecular_functionacyltransferase activity
A0016787molecular_functionhydrolase activity
A0034638biological_processphosphatidylcholine catabolic process
A0046338biological_processphosphatidylethanolamine catabolic process
A0046470biological_processphosphatidylcholine metabolic process
A0046471biological_processphosphatidylglycerol metabolic process
A0046872molecular_functionmetal ion binding
A0047499molecular_functioncalcium-independent phospholipase A2 activity
A0070062cellular_componentextracellular exosome
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Acyl-ester intermediate","evidences":[{"evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"25727495","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4X97","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Charge relay system","evidences":[{"source":"PubMed","id":"25727495","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"25727495","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"4X97","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"30830753","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"25727495","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"4X95","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"25727495","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4X90","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4X91","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4X92","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4X93","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4X94","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4X95","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4X97","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

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PDB entries from 2025-11-05

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