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1QAT

1-PHOSPHATIDYLINOSITOL-4,5-BISPHOSPHATE PHOSPHODIESTERASE DELTA COMPLEX WITH SAMARIUM (III) CHLORIDE

Functional Information from GO Data
ChainGOidnamespacecontents
A0004435molecular_functionphosphatidylinositol-4,5-bisphosphate phospholipase C activity
A0005509molecular_functioncalcium ion binding
A0006629biological_processlipid metabolic process
A0007165biological_processsignal transduction
A0008081molecular_functionphosphoric diester hydrolase activity
A0035556biological_processintracellular signal transduction
B0004435molecular_functionphosphatidylinositol-4,5-bisphosphate phospholipase C activity
B0005509molecular_functioncalcium ion binding
B0006629biological_processlipid metabolic process
B0007165biological_processsignal transduction
B0008081molecular_functionphosphoric diester hydrolase activity
B0035556biological_processintracellular signal transduction
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SM A 1001
ChainResidue
AILE651
AASP653
AASN677

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SM B 1002
ChainResidue
BILE651
BASP653
BASN677
BSM1003

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SM B 1003
ChainResidue
BTYR707
BASP708
BSM1002
BASP653
BASP706

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SM A 1004
ChainResidue
AASN312
AGLU341
AASP343
AGLU390

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SM B 1005
ChainResidue
BASN312
BGLU341
BASP343
BGLU390

Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DKNKDNKMNfkEL
ChainResidueDetails
AASP153-LEU165
AASP189-ILE201

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues288
DetailsDomain: {"description":"PI-PLC X-box","evidences":[{"source":"PROSITE-ProRule","id":"PRU00270","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues117
DetailsDomain: {"description":"PI-PLC Y-box","evidences":[{"source":"PROSITE-ProRule","id":"PRU00271","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues256
DetailsDomain: {"description":"C2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00041","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsActive site: {}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues28
DetailsBinding site: {}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 2isd
ChainResidueDetails
AHIS356
AHIS311
AGLU341

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 2isd
ChainResidueDetails
BHIS356
BHIS311
BGLU341

site_idMCSA1
Number of Residues6
DetailsM-CSA 28
ChainResidueDetails
AHIS311electrostatic stabiliser, hydrogen bond donor
AASN312metal ligand
AGLU341electrostatic stabiliser, hydrogen bond acceptor, increase acidity, metal ligand
AASP343metal ligand
AHIS356hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AGLU390hydrogen bond acceptor, hydrogen bond donor, increase acidity, metal ligand, proton acceptor, proton donor

site_idMCSA2
Number of Residues6
DetailsM-CSA 28
ChainResidueDetails
BHIS311electrostatic stabiliser, hydrogen bond donor
BASN312metal ligand
BGLU341electrostatic stabiliser, hydrogen bond acceptor, increase acidity, metal ligand
BASP343metal ligand
BHIS356hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
BGLU390hydrogen bond acceptor, hydrogen bond donor, increase acidity, metal ligand, proton acceptor, proton donor

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PDB entries from 2025-10-08

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