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2VU0

Biosynthetic thiolase from Z. ramigera. Complex of the oxidised enzyme with coenzyme A.

Functional Information from GO Data
ChainGOidnamespacecontents
A0003985molecular_functionacetyl-CoA C-acetyltransferase activity
A0003988molecular_functionacetyl-CoA C-acyltransferase activity
A0005737cellular_componentcytoplasm
A0016740molecular_functiontransferase activity
A0016746molecular_functionacyltransferase activity
A0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
A0042619biological_processpoly-hydroxybutyrate biosynthetic process
A0044281biological_processsmall molecule metabolic process
B0003985molecular_functionacetyl-CoA C-acetyltransferase activity
B0003988molecular_functionacetyl-CoA C-acyltransferase activity
B0005737cellular_componentcytoplasm
B0016740molecular_functiontransferase activity
B0016746molecular_functionacyltransferase activity
B0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
B0042619biological_processpoly-hydroxybutyrate biosynthetic process
B0044281biological_processsmall molecule metabolic process
C0003985molecular_functionacetyl-CoA C-acetyltransferase activity
C0003988molecular_functionacetyl-CoA C-acyltransferase activity
C0005737cellular_componentcytoplasm
C0016740molecular_functiontransferase activity
C0016746molecular_functionacyltransferase activity
C0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
C0042619biological_processpoly-hydroxybutyrate biosynthetic process
C0044281biological_processsmall molecule metabolic process
D0003985molecular_functionacetyl-CoA C-acetyltransferase activity
D0003988molecular_functionacetyl-CoA C-acyltransferase activity
D0005737cellular_componentcytoplasm
D0016740molecular_functiontransferase activity
D0016746molecular_functionacyltransferase activity
D0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
D0042619biological_processpoly-hydroxybutyrate biosynthetic process
D0044281biological_processsmall molecule metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues20
DetailsBINDING SITE FOR RESIDUE COA A1393
ChainResidue
ALEU148
AALA243
ASER247
AMET288
APHE319
AHIS348
AHOH2285
AHOH2287
AHOH2394
AHOH2396
CLYS208
AHIS156
DMET134
AMET157
AGLN183
AARG220
ASER227
AMET228
ALEU231
APHE235

site_idAC2
Number of Residues16
DetailsBINDING SITE FOR RESIDUE COA B1393
ChainResidue
BLEU148
BHIS156
BMET157
BARG220
BSER227
BMET228
BALA243
BGLY244
BSER247
BPHE319
BHIS348
BHOH2171
BHOH2272
BHOH2276
BHOH2279
BHOH2388

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A1394
ChainResidue
ALYS306
AILE307
AHOH2397
AHOH2398

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A1395
ChainResidue
ALYS298
AARG302
AHOH2330
AHOH2399
AHOH2400

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B1394
ChainResidue
BSER260
BALA262
BARG266

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A1396
ChainResidue
ASER260
AARG266

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B1395
ChainResidue
BLYS298
BARG302
BHOH2391

Functional Information from PROSITE/UniProt
site_idPS00098
Number of Residues19
DetailsTHIOLASE_1 Thiolases acyl-enzyme intermediate signature. MNQlCGSGLrAValgmqqI
ChainResidueDetails
AMET85-ILE103

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

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Acyl-thioester intermediate
ChainResidueDetails
ACSO89
BCSO89
CCSO89
DCSO89

site_idSWS_FT_FI2
Number of Residues8
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
AHIS348
ACYS378
BHIS348
BCYS378
CHIS348
CCYS378
DHIS348
DCYS378

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1afw
ChainResidueDetails
AHIS348
AGLY380
ACYS378

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1afw
ChainResidueDetails
BHIS348
BGLY380
BCYS378

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1afw
ChainResidueDetails
CHIS348
CGLY380
CCYS378

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1afw
ChainResidueDetails
DHIS348
DGLY380
DCYS378

site_idCSA5
Number of Residues2
DetailsAnnotated By Reference To The Literature 1afw
ChainResidueDetails
AHIS348
ACYS378

site_idCSA6
Number of Residues2
DetailsAnnotated By Reference To The Literature 1afw
ChainResidueDetails
BHIS348
BCYS378

site_idCSA7
Number of Residues2
DetailsAnnotated By Reference To The Literature 1afw
ChainResidueDetails
CHIS348
CCYS378

site_idCSA8
Number of Residues2
DetailsAnnotated By Reference To The Literature 1afw
ChainResidueDetails
DHIS348
DCYS378

237735

PDB entries from 2025-06-18

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