Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

6KZ8

Crystal structure of plant Phospholipase D alpha complex with phosphatidic acid

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004620molecular_functionphospholipase activity
A0004630molecular_functionphospholipase D 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
A0005783cellular_componentendoplasmic reticulum
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006631biological_processfatty acid metabolic 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_functionphospholipase activity
B0004630molecular_functionphospholipase D 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
B0005783cellular_componentendoplasmic reticulum
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006631biological_processfatty acid metabolic 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 Residues12
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU00153
ChainResidueDetails
AHIS332
BHIS661
BLYS663
BASP668
ALYS334
AASP339
AHIS661
ALYS663
AASP668
BHIS332
BLYS334
BASP339

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:31619765, ECO:0007744|PDB:6KZ8, ECO:0007744|PDB:6KZ9
ChainResidueDetails
AASP187
AHIS372
AHIS406
AGLU722
BASP187
BHIS372
BHIS406
BGLU722

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:31619765, ECO:0007744|PDB:6KZ8
ChainResidueDetails
AHIS332
AGLN522
AHIS661
BHIS332
BGLN522
BHIS661

222624

PDB entries from 2024-07-17

PDB statisticsPDBj update infoContact PDBjnumon