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4XL2

Crystal structure of oxidized form of thiolase from Clostridium acetobutylicum

Functional Information from GO Data
ChainGOidnamespacecontents
A0003985molecular_functionacetyl-CoA C-acetyltransferase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006635biological_processfatty acid beta-oxidation
A0016740molecular_functiontransferase activity
A0016746molecular_functionacyltransferase activity
A0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
B0003985molecular_functionacetyl-CoA C-acetyltransferase activity
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006635biological_processfatty acid beta-oxidation
B0016740molecular_functiontransferase activity
B0016746molecular_functionacyltransferase activity
B0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
Functional Information from PDB Data
site_idAC1
Number of Residues7
Detailsbinding site for residue ACT A 501
ChainResidue
ASER96
AGLY279
ASER280
ATHR385
AALA386
AILE387
AHOH746

site_idAC2
Number of Residues5
Detailsbinding site for residue PEG A 502
ChainResidue
AGLY268
ALYS270
ALYS302
ALYS265
AGLU266

site_idAC3
Number of Residues5
Detailsbinding site for residue PEG A 503
ChainResidue
ATRP130
AARG133
AHOH679
AHOH696
BLYS22

site_idAC4
Number of Residues4
Detailsbinding site for residue PEG A 504
ChainResidue
AASP28
ATHR32
ALYS35
AHOH720

site_idAC5
Number of Residues5
Detailsbinding site for residue PEG A 505
ChainResidue
ALEU324
AALA327
APHE332
AMET334
AHOH753

site_idAC6
Number of Residues7
Detailsbinding site for residue GOL A 506
ChainResidue
ALEU148
ASER247
AGLY248
AALA318
AHIS348
AHOH651
AHOH817

site_idAC7
Number of Residues7
Detailsbinding site for residue ACT B 501
ChainResidue
BSER96
BGLY279
BSER280
BTHR385
BALA386
BILE387
BHOH709

site_idAC8
Number of Residues3
Detailsbinding site for residue PEG B 502
ChainResidue
BTRP130
BHOH657
BHOH738

site_idAC9
Number of Residues4
Detailsbinding site for residue PEG B 503
ChainResidue
ALYS138
BALA137
BLYS138
BHOH623

site_idAD1
Number of Residues4
Detailsbinding site for residue PEG B 504
ChainResidue
BASP28
BTHR32
BLYS35
BHOH688

site_idAD2
Number of Residues2
Detailsbinding site for residue PEG B 505
ChainResidue
ATYR17
BARG133

site_idAD3
Number of Residues6
Detailsbinding site for residue GOL B 506
ChainResidue
BLEU148
BSER247
BALA318
BHIS348
BHOH652
BHOH813

Functional Information from PROSITE/UniProt
site_idPS00098
Number of Residues19
DetailsTHIOLASE_1 Thiolases acyl-enzyme intermediate signature. INKvCGSGLrTVslaaqiI
ChainResidueDetails
AILE84-ILE102

site_idPS00099
Number of Residues14
DetailsTHIOLASE_3 Thiolases active site. GLATLCIGgGqGtA
ChainResidueDetails
AGLY373-ALA386

site_idPS00737
Number of Residues17
DetailsTHIOLASE_2 Thiolases signature 2. NvnGGaIAlGHPiGaSG
ChainResidueDetails
AASN338-GLY354

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Acyl-thioester intermediate => ECO:0000305|PubMed:26391388
ChainResidueDetails
ACYS88
BCYS88

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:26391388
ChainResidueDetails
AHIS348
ACYS378
BHIS348
BCYS378

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:26391388, ECO:0007744|PDB:4XL2
ChainResidueDetails
ASER96
AGLY279
AALA386
BSER96
BGLY279
BALA386

218853

PDB entries from 2024-04-24

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