Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

1WL5

Human cytosolic acetoacetyl-CoA thiolase

Functional Information from GO Data
ChainGOidnamespacecontents
A0003985molecular_functionacetyl-CoA C-acetyltransferase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006629biological_processlipid metabolic process
A0006631biological_processfatty acid metabolic process
A0010142biological_processfarnesyl diphosphate biosynthetic process, mevalonate pathway
A0016740molecular_functiontransferase activity
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
DetailsActive site: {"description":"Acyl-thioester intermediate","evidences":[{"source":"PubMed","id":"15733928","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"15733928","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15733928","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1WL4","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsSite: {"description":"Increases nucleophilicity of active site Cys","evidences":[{"source":"UniProtKB","id":"P42765","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues3
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

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

245663

PDB entries from 2025-12-03

PDB statisticsPDBj update infoContact PDBjnumon