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2VU1

Biosynthetic thiolase from Z. ramigera. Complex of with O-pantheteine- 11-pivalate.

Functional Information from GO Data
ChainGOidnamespacecontents
A0003985molecular_functionacetyl-CoA C-acetyltransferase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006635biological_processfatty acid beta-oxidation
A0016746molecular_functionacyltransferase activity
A0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
A0042619biological_processpoly-hydroxybutyrate biosynthetic process
B0003985molecular_functionacetyl-CoA C-acetyltransferase activity
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006635biological_processfatty acid beta-oxidation
B0016746molecular_functionacyltransferase activity
B0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
B0042619biological_processpoly-hydroxybutyrate biosynthetic process
C0003985molecular_functionacetyl-CoA C-acetyltransferase activity
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006635biological_processfatty acid beta-oxidation
C0016746molecular_functionacyltransferase activity
C0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
C0042619biological_processpoly-hydroxybutyrate biosynthetic process
D0003985molecular_functionacetyl-CoA C-acetyltransferase activity
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006635biological_processfatty acid beta-oxidation
D0016746molecular_functionacyltransferase activity
D0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
D0042619biological_processpoly-hydroxybutyrate biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE OPI A1393
ChainResidue
AHIS156
APHE235
ASER247
AALA318
AHIS348
AHOH2405
DMET134

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE NA A1394
ChainResidue
AGLU29
AHOH2042

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A1395
ChainResidue
ASER260
AALA262
AARG266

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A1396
ChainResidue
ALYS298
AARG302
AHOH2339
AHOH2408
BGLY106

site_idAC5
Number of Residues12
DetailsBINDING SITE FOR RESIDUE OPI B1393
ChainResidue
BPHE235
BALA243
BSER247
BGLY248
BLEU249
BALA318
BPHE319
BHIS348
BHOH2282
BHOH2389
BHOH2390
CMET134

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B1394
ChainResidue
BLYS298
BARG302
BHOH2391
BHOH2392

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 B1395
ChainResidue
BSER260
BALA262
BARG266
BHOH2292
BHOH2396
BHOH2397
BHOH2398

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 D1393
ChainResidue
DARG194
DGLU364
DARG367

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B1394
ChainResidue
BLYS298
BARG302
BHOH2391
BHOH2392

site_idBC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A1395
ChainResidue
ASER260
AALA262
AARG266

site_idBC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 B1395
ChainResidue
BSER260
BALA262
BARG266
BHOH2292
BHOH2396
BHOH2397
BHOH2398

site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A1396
ChainResidue
ALYS298
AARG302
AHOH2339
AHOH2408
BGLY106

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

219140

PDB entries from 2024-05-01

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