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1WL5

Human cytosolic acetoacetyl-CoA thiolase

Functional Information from GO Data
ChainGOidnamespacecontents
A0003985molecular_functionacetyl-CoA C-acetyltransferase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005829cellular_componentcytosol
A0006629biological_processlipid metabolic process
A0006631biological_processfatty acid metabolic process
A0006635biological_processfatty acid beta-oxidation
A0016746molecular_functionacyltransferase activity
A0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
A0070062cellular_componentextracellular exosome
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SO4 A 1001
ChainResidue
ASER12
AHOH2169
AALA13
AARG44
ALEU277
AASN338
AHIS368
AHOH2109
AHOH2144
AHOH2149

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 1002
ChainResidue
ATYR81
AHIS156
AGLU289
APRO290
ASER291
AHOH2133

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 1003
ChainResidue
AGLU215
ALYS217
ATHR218
AHOH2232

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE GOL A 2001
ChainResidue
ALEU151
AGLY253

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 2002
ChainResidue
ALEU184
AGLU322
AVAL332
AASN343
AHOH2241

Functional Information from PROSITE/UniProt
site_idPS00099
Number of Residues14
DetailsTHIOLASE_3 Thiolases active site. GVAALCIGgGmGiA
ChainResidueDetails
AGLY378-ALA391

site_idPS00737
Number of Residues17
DetailsTHIOLASE_2 Thiolases signature 2. NieGGaIAlGHPlGaSG
ChainResidueDetails
AASN343-GLY359

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Acyl-thioester intermediate => ECO:0000305|PubMed:15733928
ChainResidueDetails
ACSO92

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor/acceptor => ECO:0000305|PubMed:15733928
ChainResidueDetails
ACYS383

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:15733928, ECO:0007744|PDB:1WL4
ChainResidueDetails
AARG223
ASER226
ASER252

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Increases nucleophilicity of active site Cys => ECO:0000250|UniProtKB:P42765
ChainResidueDetails
AHIS353

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: N-acetylmethionine => ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378
ChainResidueDetails
AMET1

site_idSWS_FT_FI6
Number of Residues3
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS200
ALYS233
ALYS235

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1afw
ChainResidueDetails
AHIS353
ACYS383
AGLY385

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1afw
ChainResidueDetails
AHIS353
ACYS383

223532

PDB entries from 2024-08-07

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