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2WKU

BIOSYNTHETIC THIOLASE FROM Z. RAMIGERA. THE N316H MUTANT.

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 Residues2
DetailsBINDING SITE FOR RESIDUE SO4 B 1393
ChainResidue
BSER260
BARG266

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 B 1394
ChainResidue
BLYS298
BARG302

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 1393
ChainResidue
AHOH2187
AARG41
AILE199
APRO201
ADNO1396
AHOH2186

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 B 1398
ChainResidue
BHOH2213
BHOH2214

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 1395
ChainResidue
BMET72
BLYS73
BGLY75

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 1394
ChainResidue
ASER260
AARG266

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 C 1393
ChainResidue
CARG41
CVAL200
CHOH2014
CHOH2113
CHOH2115

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 1396
ChainResidue
BARG220
BHIS221
BHOH2211

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 1395
ChainResidue
AARG220
AHIS221
AHOH2189

site_idBC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE DNO A 1396
ChainResidue
AALA8
ASER9
AALA10
AARG41
AASP197
ALEU272
APHE363
ASO41393
AHOH2190
AHOH2191
AHOH2192

site_idBC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE DNO A 1397
ChainResidue
ALYS185
APRO334
ASER335
AVAL337
AVAL339
AARG368
AHOH2173

site_idBC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE DNO B 1397
ChainResidue
BALA8
BSER9
BALA10
BARG41
BASP197
BLEU272
BPHE363
BHOH2030

site_idBC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE DNO A 1398
ChainResidue
AVAL283
AASP284
ATHR290
AHOH2193
AHOH2194
AHOH2195
BGLN78

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
DetailsActive site: {"description":"Acyl-thioester intermediate"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues8
DetailsActive site: {"description":"Proton acceptor"}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1afw
ChainResidueDetails
AHIS348
AGLY380
ACYS378
ACYS89

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1afw
ChainResidueDetails
BHIS348
BGLY380
BCYS378
BCYS89

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1afw
ChainResidueDetails
CHIS348
CGLY380
CCYS378
CCYS89

site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1afw
ChainResidueDetails
DHIS348
DGLY380
DCYS378
DCYS89

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

238895

PDB entries from 2025-07-16

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