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7SVP

Structure of compound 34 bound to human Phospholipase D2 catalytic domain

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004630molecular_functionD-type glycerophospholipase activity
A0006654biological_processphosphatidic acid biosynthetic process
A0035556biological_processintracellular signal transduction
B0003824molecular_functioncatalytic activity
B0004630molecular_functionD-type glycerophospholipase activity
B0006654biological_processphosphatidic acid biosynthetic process
B0035556biological_processintracellular signal transduction
C0003824molecular_functioncatalytic activity
C0004630molecular_functionD-type glycerophospholipase activity
C0006654biological_processphosphatidic acid biosynthetic process
C0035556biological_processintracellular signal transduction
D0003824molecular_functioncatalytic activity
D0004630molecular_functionD-type glycerophospholipase activity
D0006654biological_processphosphatidic acid biosynthetic process
D0035556biological_processintracellular signal transduction
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues108
DetailsDomain: {"description":"PLD phosphodiesterase 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00153","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues108
DetailsDomain: {"description":"PLD phosphodiesterase 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00153","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

250835

PDB entries from 2026-03-18

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