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5XYJ

Purification,crystallization and structural analysis of cytoplastic acetoacetyl-CoA thiolase from Saccharomyces cerevisiae

Functional Information from GO Data
ChainGOidnamespacecontents
A0003985molecular_functionacetyl-CoA C-acetyltransferase activity
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005773cellular_componentvacuole
A0005829cellular_componentcytosol
A0006635biological_processfatty acid beta-oxidation
A0006696biological_processergosterol biosynthetic process
A0016746molecular_functionacyltransferase activity
A0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
A0046872molecular_functionmetal ion binding
B0003985molecular_functionacetyl-CoA C-acetyltransferase activity
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005773cellular_componentvacuole
B0005829cellular_componentcytosol
B0006635biological_processfatty acid beta-oxidation
B0006696biological_processergosterol biosynthetic process
B0016746molecular_functionacyltransferase activity
B0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues7
Detailsbinding site for residue GOL B 401
ChainResidue
BLEU151
BSER252
BPHE325
BHIS354
BHOH543
BHOH638
BHOH777

site_idAC2
Number of Residues9
Detailsbinding site for residue GOL A 401
ChainResidue
APHE325
AHIS354
AHOH520
AHOH537
AHOH558
AHOH564
AHOH739
ALEU151
ASER252

Functional Information from PROSITE/UniProt
site_idPS00099
Number of Residues14
DetailsTHIOLASE_3 Thiolases active site. GVAAICNGgGgAsS
ChainResidueDetails
BGLY379-SER392

site_idPS00737
Number of Residues17
DetailsTHIOLASE_2 Thiolases signature 2. NvyGGaVAlGHPlGcSG
ChainResidueDetails
BASN344-GLY360

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Acyl-thioester intermediate => ECO:0000250|UniProtKB:P24752
ChainResidueDetails
BALA91
AALA91

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10020
ChainResidueDetails
BHIS354
BCYS384
AHIS354
ACYS384

site_idSWS_FT_FI3
Number of Residues14
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P24752
ChainResidueDetails
BALA248
BALA249
BALA251
BSER252
BVAL350
ATYR186
ALYS231
AALA248
AALA249
AALA251
ASER252
AVAL350
BLYS231
BTYR186

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N-acetylserine => ECO:0000269|Ref.4, ECO:0007744|PubMed:22814378
ChainResidueDetails
BSER2
ASER2

219869

PDB entries from 2024-05-15

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