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2ISD

PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C-DELTA1 FROM RAT

Replaces:  1ISD
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
A0035556biological_processintracellular signal transduction
B0004435molecular_functionphosphatidylinositol 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 Residues6
DetailsBINDING SITE FOR RESIDUE ACT A 5
ChainResidue
AGLY583
APRO584
AASP587
AARG701
APHE715
ALYS738

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ACT B 5
ChainResidue
BARG701
BPHE715
BLYS738
BHOH997
BGLY583
BPRO584
BASP587

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 Residues4
DetailsACT_SITE:
ChainResidueDetails
AHIS311
AHIS356
BHIS311
BHIS356

site_idSWS_FT_FI2
Number of Residues20
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448
ChainResidueDetails
AASP153
AGLU200
BASP153
BASN155
BASP157
BLYS159
BGLU164
BASP189
BSER191
BTHR193
BSER195
AASN155
BGLU200
AASP157
ALYS159
AGLU164
AASP189
ASER191
ATHR193
ASER195

site_idSWS_FT_FI3
Number of Residues28
DetailsBINDING:
ChainResidueDetails
AASN312
AASP653
AASN677
AASP706
ATYR707
AASP708
BASN312
BGLU341
BASP343
BGLU390
BLYS438
AGLU341
BLYS440
BSER522
BARG549
BILE651
BASP653
BASN677
BASP706
BTYR707
BASP708
AASP343
AGLU390
ALYS438
ALYS440
ASER522
AARG549
AILE651

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q8R3B1
ChainResidueDetails
ATHR457
BTHR457

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P51178
ChainResidueDetails
ASER460
BSER460

site_idSWS_FT_FI6
Number of Residues2
DetailsCARBOHYD: O-linked (GlcNAc) serine => ECO:0000269|PubMed:24098488
ChainResidueDetails
ASER191
BSER191

site_idSWS_FT_FI7
Number of Residues2
DetailsCARBOHYD: O-linked (GlcNAc) threonine => ECO:0000269|PubMed:24098488
ChainResidueDetails
ATHR193
BTHR193

Catalytic Information from CSA
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 2024-04-24

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