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6KZ8

Crystal structure of plant Phospholipase D alpha complex with phosphatidic acid

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004620molecular_functionglycerophospholipase activity
A0004630molecular_functionD-type glycerophospholipase activity
A0005096molecular_functionGTPase activator activity
A0005509molecular_functioncalcium ion binding
A0005515molecular_functionprotein binding
A0005546molecular_functionphosphatidylinositol-4,5-bisphosphate binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005773cellular_componentvacuole
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006629biological_processlipid metabolic process
A0006631biological_processfatty acid metabolic process
A0009395biological_processphospholipid catabolic process
A0009506cellular_componentplasmodesma
A0009507cellular_componentchloroplast
A0009737biological_processresponse to abscisic acid
A0009738biological_processabscisic acid-activated signaling pathway
A0009789biological_processpositive regulation of abscisic acid-activated signaling pathway
A0009845biological_processseed germination
A0009873biological_processethylene-activated signaling pathway
A0010119biological_processregulation of stomatal movement
A0010358biological_processleaf shaping
A0016020cellular_componentmembrane
A0016042biological_processlipid catabolic process
A0016787molecular_functionhydrolase activity
A0030136cellular_componentclathrin-coated vesicle
A0031410cellular_componentcytoplasmic vesicle
A0031966cellular_componentmitochondrial membrane
A0046470biological_processphosphatidylcholine metabolic process
A0046872molecular_functionmetal ion binding
B0003824molecular_functioncatalytic activity
B0004620molecular_functionglycerophospholipase activity
B0004630molecular_functionD-type glycerophospholipase activity
B0005096molecular_functionGTPase activator activity
B0005509molecular_functioncalcium ion binding
B0005515molecular_functionprotein binding
B0005546molecular_functionphosphatidylinositol-4,5-bisphosphate binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005773cellular_componentvacuole
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006629biological_processlipid metabolic process
B0006631biological_processfatty acid metabolic process
B0009395biological_processphospholipid catabolic process
B0009506cellular_componentplasmodesma
B0009507cellular_componentchloroplast
B0009737biological_processresponse to abscisic acid
B0009738biological_processabscisic acid-activated signaling pathway
B0009789biological_processpositive regulation of abscisic acid-activated signaling pathway
B0009845biological_processseed germination
B0009873biological_processethylene-activated signaling pathway
B0010119biological_processregulation of stomatal movement
B0010358biological_processleaf shaping
B0016020cellular_componentmembrane
B0016042biological_processlipid catabolic process
B0016787molecular_functionhydrolase activity
B0030136cellular_componentclathrin-coated vesicle
B0031410cellular_componentcytoplasmic vesicle
B0031966cellular_componentmitochondrial membrane
B0046470biological_processphosphatidylcholine metabolic process
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues18
Detailsbinding site for residue PA8 A 1101
ChainResidue
ATRP231
ASER583
AVAL584
AILE587
AHIS661
AARG682
AASP689
ALEU808
AHOH1207
AHOH1338
ATHR330
AHIS332
AARG366
AGLN522
ATYR523
APRO575
AGLU576
ASER581

site_idAC2
Number of Residues4
Detailsbinding site for residue CA A 1102
ChainResidue
AASP187
AHIS372
AHIS406
AGLU722

site_idAC3
Number of Residues4
Detailsbinding site for residue CA B 901
ChainResidue
BASP187
BHIS372
BHIS406
BGLU722

site_idAC4
Number of Residues17
Detailsbinding site for residue PA8 B 902
ChainResidue
BTRP231
BTHR330
BHIS332
BARG366
BGLN522
BTYR523
BGLU576
BSER581
BSER583
BVAL584
BILE587
BHIS661
BARG682
BASP689
BLEU808
BHOH1040
BHOH1087

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues78
DetailsDomain: {"description":"PLD phosphodiesterase 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00153","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues54
DetailsDomain: {"description":"PLD phosphodiesterase 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00153","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues12
DetailsActive site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00153","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"31619765","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6KZ8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6KZ9","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"31619765","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6KZ8","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

249697

PDB entries from 2026-02-25

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