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2ZKM

Crystal Structure of Phospholipase C Beta 2

Functional Information from GO Data
ChainGOidnamespacecontents
X0004435molecular_functionphosphatidylinositol-4,5-bisphosphate phospholipase C activity
X0004629molecular_functionphospholipase C activity
X0006629biological_processlipid metabolic process
X0007165biological_processsignal transduction
X0008081molecular_functionphosphoric diester hydrolase activity
X0035556biological_processintracellular signal transduction
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA X 800
ChainResidue
XASN328
XGLU357
XASP359
XGLU408
XHOH842
XHOH844

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues151
DetailsDomain: {"description":"PI-PLC X-box","evidences":[{"source":"PROSITE-ProRule","id":"PRU00270","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues116
DetailsDomain: {"description":"PI-PLC Y-box","evidences":[{"source":"PROSITE-ProRule","id":"PRU00271","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues128
DetailsDomain: {"description":"C2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00041","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsActive site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00270","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
DetailsBinding site: {}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 2isd
ChainResidueDetails
XHIS374
XGLU357
XHIS327

246704

PDB entries from 2025-12-24

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