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7Z3J

Structure of crystallisable rat Phospholipase C gamma 1 in complex with inositol 1,4,5-trisphosphate

Functional Information from GO Data
ChainGOidnamespacecontents
A0004435molecular_functionphosphatidylinositol phospholipase C activity
A0005509molecular_functioncalcium ion binding
A0006629biological_processlipid metabolic process
A0007165biological_processsignal transduction
A0008081molecular_functionphosphoric diester hydrolase activity
A0009395biological_processphospholipid catabolic process
A0035556biological_processintracellular signal transduction
Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DRNREDRISakDL
ChainResidueDetails
AASP165-LEU177

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU00270
ChainResidueDetails
AHIS335
AHIS380

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448
ChainResidueDetails
AASP165
AASN167
AGLU169
AARG171
AASP176

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q62077
ChainResidueDetails
ATYR506
ATYR977

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by SYK => ECO:0000250|UniProtKB:P08487
ChainResidueDetails
ALYS793

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P19174
ChainResidueDetails
ALYS797

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by ITK, SYK and TXK => ECO:0000250|UniProtKB:P19174
ChainResidueDetails
AGLN805

224572

PDB entries from 2024-09-04

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