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5XZ5

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 PROSITE/UniProt
site_idPS00098
Number of Residues19
DetailsTHIOLASE_1 Thiolases acyl-enzyme intermediate signature. VNKvCASAMkAIilgaqsI
ChainResidueDetails
AVAL87-ILE105

site_idPS00099
Number of Residues14
DetailsTHIOLASE_3 Thiolases active site. GVAAICNGgGgAsS
ChainResidueDetails
AGLY379-SER392

site_idPS00737
Number of Residues17
DetailsTHIOLASE_2 Thiolases signature 2. NvyGGaVAlGHPlGcSG
ChainResidueDetails
AASN344-GLY360

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Acyl-thioester intermediate => ECO:0000250|UniProtKB:P24752
ChainResidueDetails
ACYS91
BCYS91

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

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

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

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PDB entries from 2024-07-24

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