2WKU
BIOSYNTHETIC THIOLASE FROM Z. RAMIGERA. THE N316H MUTANT.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003985 | molecular_function | acetyl-CoA C-acetyltransferase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006635 | biological_process | fatty acid beta-oxidation |
| A | 0016746 | molecular_function | acyltransferase activity |
| A | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
| A | 0042619 | biological_process | poly-hydroxybutyrate biosynthetic process |
| B | 0003985 | molecular_function | acetyl-CoA C-acetyltransferase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006635 | biological_process | fatty acid beta-oxidation |
| B | 0016746 | molecular_function | acyltransferase activity |
| B | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
| B | 0042619 | biological_process | poly-hydroxybutyrate biosynthetic process |
| C | 0003985 | molecular_function | acetyl-CoA C-acetyltransferase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005829 | cellular_component | cytosol |
| C | 0006635 | biological_process | fatty acid beta-oxidation |
| C | 0016746 | molecular_function | acyltransferase activity |
| C | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
| C | 0042619 | biological_process | poly-hydroxybutyrate biosynthetic process |
| D | 0003985 | molecular_function | acetyl-CoA C-acetyltransferase activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005829 | cellular_component | cytosol |
| D | 0006635 | biological_process | fatty acid beta-oxidation |
| D | 0016746 | molecular_function | acyltransferase activity |
| D | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
| D | 0042619 | biological_process | poly-hydroxybutyrate biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1393 |
| Chain | Residue |
| B | SER260 |
| B | ARG266 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1394 |
| Chain | Residue |
| B | LYS298 |
| B | ARG302 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1393 |
| Chain | Residue |
| A | HOH2187 |
| A | ARG41 |
| A | ILE199 |
| A | PRO201 |
| A | DNO1396 |
| A | HOH2186 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1398 |
| Chain | Residue |
| B | HOH2213 |
| B | HOH2214 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1395 |
| Chain | Residue |
| B | MET72 |
| B | LYS73 |
| B | GLY75 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1394 |
| Chain | Residue |
| A | SER260 |
| A | ARG266 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 C 1393 |
| Chain | Residue |
| C | ARG41 |
| C | VAL200 |
| C | HOH2014 |
| C | HOH2113 |
| C | HOH2115 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1396 |
| Chain | Residue |
| B | ARG220 |
| B | HIS221 |
| B | HOH2211 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1395 |
| Chain | Residue |
| A | ARG220 |
| A | HIS221 |
| A | HOH2189 |
| site_id | BC1 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE DNO A 1396 |
| Chain | Residue |
| A | ALA8 |
| A | SER9 |
| A | ALA10 |
| A | ARG41 |
| A | ASP197 |
| A | LEU272 |
| A | PHE363 |
| A | SO41393 |
| A | HOH2190 |
| A | HOH2191 |
| A | HOH2192 |
| site_id | BC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE DNO A 1397 |
| Chain | Residue |
| A | LYS185 |
| A | PRO334 |
| A | SER335 |
| A | VAL337 |
| A | VAL339 |
| A | ARG368 |
| A | HOH2173 |
| site_id | BC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE DNO B 1397 |
| Chain | Residue |
| B | ALA8 |
| B | SER9 |
| B | ALA10 |
| B | ARG41 |
| B | ASP197 |
| B | LEU272 |
| B | PHE363 |
| B | HOH2030 |
| site_id | BC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE DNO A 1398 |
| Chain | Residue |
| A | VAL283 |
| A | ASP284 |
| A | THR290 |
| A | HOH2193 |
| A | HOH2194 |
| A | HOH2195 |
| B | GLN78 |
Functional Information from PROSITE/UniProt
| site_id | PS00098 |
| Number of Residues | 19 |
| Details | THIOLASE_1 Thiolases acyl-enzyme intermediate signature. MNQlCGSGLrAValgmqqI |
| Chain | Residue | Details |
| A | MET85-ILE103 |
| site_id | PS00099 |
| Number of Residues | 14 |
| Details | THIOLASE_3 Thiolases active site. GLATLCIGgGmGvA |
| Chain | Residue | Details |
| A | GLY373-ALA386 |
| site_id | PS00737 |
| Number of Residues | 17 |
| Details | THIOLASE_2 Thiolases signature 2. NvnGGaIAiGHPiGaSG |
| Chain | Residue | Details |
| A | ASN338-GLY354 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Acyl-thioester intermediate |
| Chain | Residue | Details |
| A | CYS89 | |
| B | CYS89 | |
| C | CYS89 | |
| D | CYS89 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | ACT_SITE: Proton acceptor |
| Chain | Residue | Details |
| A | HIS348 | |
| A | CYS378 | |
| B | HIS348 | |
| B | CYS378 | |
| C | HIS348 | |
| C | CYS378 | |
| D | HIS348 | |
| D | CYS378 |
