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2WU9

Crystal structure of peroxisomal KAT2 from Arabidopsis thaliana

Functional Information from GO Data
ChainGOidnamespacecontents
A0000325cellular_componentplant-type vacuole
A0003988molecular_functionacetyl-CoA C-acyltransferase activity
A0005515molecular_functionprotein binding
A0005730cellular_componentnucleolus
A0005739cellular_componentmitochondrion
A0005777cellular_componentperoxisome
A0005783cellular_componentendoplasmic reticulum
A0005829cellular_componentcytosol
A0006629biological_processlipid metabolic process
A0006631biological_processfatty acid metabolic process
A0006633biological_processfatty acid biosynthetic process
A0006635biological_processfatty acid beta-oxidation
A0009514cellular_componentglyoxysome
A0009611biological_processresponse to wounding
A0009695biological_processjasmonic acid biosynthetic process
A0009789biological_processpositive regulation of abscisic acid-activated signaling pathway
A0010111biological_processglyoxysome organization
A0010124biological_processphenylacetate catabolic process
A0016740molecular_functiontransferase activity
A0016746molecular_functionacyltransferase activity
A0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
A0031408biological_processoxylipin biosynthetic process
B0000325cellular_componentplant-type vacuole
B0003988molecular_functionacetyl-CoA C-acyltransferase activity
B0005515molecular_functionprotein binding
B0005730cellular_componentnucleolus
B0005739cellular_componentmitochondrion
B0005777cellular_componentperoxisome
B0005783cellular_componentendoplasmic reticulum
B0005829cellular_componentcytosol
B0006629biological_processlipid metabolic process
B0006631biological_processfatty acid metabolic process
B0006633biological_processfatty acid biosynthetic process
B0006635biological_processfatty acid beta-oxidation
B0009514cellular_componentglyoxysome
B0009611biological_processresponse to wounding
B0009695biological_processjasmonic acid biosynthetic process
B0009789biological_processpositive regulation of abscisic acid-activated signaling pathway
B0010111biological_processglyoxysome organization
B0010124biological_processphenylacetate catabolic process
B0016740molecular_functiontransferase activity
B0016746molecular_functionacyltransferase activity
B0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
B0031408biological_processoxylipin biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 1449
ChainResidue
AASP50
AHOH2595
AHOH2596

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE EDO A 1450
ChainResidue
ATHR170
AASN171
AHOH2597
APRO75
AALA107
APRO108
AGLN111
AARG112
AGLU115

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 1451
ChainResidue
AGLY155
AASP158
AHOH2255
AHOH2454

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 1452
ChainResidue
AALA217
ASER221
ALYS224
AGLU362
APHE368
AHOH2527
AHOH2599

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EDO A 1453
ChainResidue
ACYS192
ALEU194
AMET196
ATHR199
APRO330
AMET333
ATHR428
AHOH2600

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 1454
ChainResidue
AGLN216
AVAL219
ALEU270
AHOH2358
AHOH2601
BHOH2531

site_idAC7
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EDO B 1449
ChainResidue
BALA217
BASP220
BSER221
BLYS224
BGLU362
BPHE368
BHOH2297
BHOH2532

site_idAC8
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EDO B 1450
ChainResidue
BLEU47
BARG306
BVAL316
BVAL319
BARG321
BGLY439
BASP440
BGLU444

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO B 1451
ChainResidue
APHE156
BTHR322
BPHE323
BALA347
BHOH2424
BHOH2533

Functional Information from PROSITE/UniProt
site_idPS00098
Number of Residues19
DetailsTHIOLASE_1 Thiolases acyl-enzyme intermediate signature. VNRqCSSGLqAVadvaaaI
ChainResidueDetails
AVAL134-ILE152

site_idPS00099
Number of Residues14
DetailsTHIOLASE_3 Thiolases active site. GVVSMCIGtGmGaA
ChainResidueDetails
AGLY420-ALA433

site_idPS00737
Number of Residues17
DetailsTHIOLASE_2 Thiolases signature 2. NvnGGaMAiGHPlGaTG
ChainResidueDetails
AASN383-GLY399

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Acyl-thioester intermediate => ECO:0000250
ChainResidueDetails
ACYS138
BCYS138

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10020
ChainResidueDetails
AHIS393
ACYS425
BHIS393
BCYS425

237992

PDB entries from 2025-06-25

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