2WKT
BIOSYNTHETIC THIOLASE FROM Z. RAMIGERA. COMPLEX OF THE N316A MUTANT WITH COENZYME A.
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 | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1393 |
| Chain | Residue |
| A | SER260 |
| A | ALA262 |
| A | ARG266 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1393 |
| Chain | Residue |
| B | HOH2414 |
| B | HOH2415 |
| B | SER260 |
| B | GLU263 |
| B | ARG266 |
| B | HOH2162 |
| B | HOH2412 |
| B | HOH2413 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1394 |
| Chain | Residue |
| B | LYS298 |
| B | ARG302 |
| B | HOH2344 |
| B | HOH2416 |
| B | HOH2417 |
| B | HOH2418 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1394 |
| Chain | Residue |
| A | LYS298 |
| A | GLU301 |
| A | ARG302 |
| A | HOH2432 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 D 1393 |
| Chain | Residue |
| D | LYS298 |
| D | ARG302 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1395 |
| Chain | Residue |
| B | GLN167 |
| B | TRP168 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 D 1394 |
| Chain | Residue |
| D | ARG41 |
| D | ILE199 |
| D | VAL200 |
| D | PRO201 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1396 |
| Chain | Residue |
| B | ARG41 |
| B | VAL200 |
| B | HOH2057 |
| B | HOH2251 |
| B | HOH2421 |
| B | HOH2422 |
| B | HOH2423 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1397 |
| Chain | Residue |
| B | ARG368 |
| B | HOH2384 |
| site_id | BC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE K A 1395 |
| Chain | Residue |
| A | GLN56 |
| A | CL1396 |
| B | HOH2127 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA C 1393 |
| Chain | Residue |
| C | VAL52 |
| C | ILE53 |
| C | LEU54 |
| C | ALA67 |
| C | TRP83 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CL A 1396 |
| Chain | Residue |
| A | LEU54 |
| A | GLY55 |
| A | GLN56 |
| A | GLY84 |
| A | MET85 |
| A | K1395 |
| site_id | BC4 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE COA A 1397 |
| Chain | Residue |
| A | CSO89 |
| A | LEU148 |
| A | HIS156 |
| A | MET157 |
| A | ARG220 |
| A | SER227 |
| A | MET228 |
| A | LEU231 |
| A | PHE235 |
| A | GLY244 |
| A | SER247 |
| A | MET288 |
| A | PHE319 |
| A | HIS348 |
| A | HOH2289 |
| A | HOH2300 |
| A | HOH2322 |
| A | HOH2324 |
| A | HOH2325 |
| A | HOH2434 |
| A | HOH2435 |
| A | HOH2436 |
| A | HOH2439 |
| A | HOH2440 |
| C | LYS208 |
| D | LYS133 |
| site_id | BC5 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE COA B 1398 |
| Chain | Residue |
| B | HOH2424 |
| B | HOH2425 |
| B | HOH2426 |
| B | HOH2427 |
| B | HOH2428 |
| B | HOH2429 |
| B | HOH2430 |
| C | MET134 |
| B | CSO89 |
| B | LEU148 |
| B | HIS156 |
| B | MET157 |
| B | ARG220 |
| B | SER227 |
| B | MET228 |
| B | LEU231 |
| B | PHE235 |
| B | ALA243 |
| B | GLY244 |
| B | SER247 |
| B | LEU249 |
| B | MET288 |
| B | PHE319 |
| B | HOH2282 |
| B | HOH2284 |
| B | HOH2290 |
| B | HOH2306 |
| B | HOH2307 |
| B | HOH2309 |
| site_id | BC6 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE COA C 1394 |
| Chain | Residue |
| A | LYS208 |
| C | CYS89 |
| C | LEU148 |
| C | HIS156 |
| C | MET157 |
| C | ARG220 |
| C | SER227 |
| C | MET228 |
| C | LEU231 |
| C | ALA243 |
| C | GLY244 |
| C | SER247 |
| C | MET288 |
| C | ALA318 |
| C | PHE319 |
| C | HOH2170 |
| C | HOH2182 |
| C | HOH2183 |
| C | HOH2254 |
| site_id | BC7 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE COA D 1395 |
| Chain | Residue |
| A | MET134 |
| D | CSO89 |
| D | LEU148 |
| D | HIS156 |
| D | MET157 |
| D | ARG220 |
| D | SER227 |
| D | LEU231 |
| D | PHE235 |
| D | ALA243 |
| D | GLY244 |
| D | SER247 |
| D | GLY248 |
| D | LEU249 |
| D | MET288 |
| D | ALA318 |
| D | PHE319 |
| D | HIS348 |
| D | HOH2114 |
| D | HOH2164 |
| D | HOH2165 |
| D | HOH2196 |
| D | HOH2215 |
| D | HOH2216 |
| D | HOH2218 |
Functional Information from PROSITE/UniProt
| site_id | PS00098 |
| Number of Residues | 19 |
| Details | THIOLASE_1 Thiolases acyl-enzyme intermediate signature. MNQlCGSGLrAValgmqqI |
| Chain | Residue | Details |
| C | MET85-ILE103 | |
| A | MET85-ILE103 |
| site_id | PS00099 |
| Number of Residues | 14 |
| Details | THIOLASE_3 Thiolases active site. GLATLCIGgGmGvA |
| Chain | Residue | Details |
| C | GLY373-ALA386 | |
| A | GLY373-ALA386 |
| site_id | PS00737 |
| Number of Residues | 17 |
| Details | THIOLASE_2 Thiolases signature 2. NvnGGaIAiGHPiGaSG |
| Chain | Residue | Details |
| C | ASN338-GLY354 | |
| A | ASN338-GLY354 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | ACT_SITE: Acyl-thioester intermediate |
| Chain | Residue | Details |
| C | CYS89 | |
| B | CSO89 | |
| D | CSO89 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor |
| Chain | Residue | Details |
| C | HIS348 | |
| C | CYS378 | |
| B | HIS348 | |
| B | CYS378 | |
| D | HIS348 | |
| D | CYS378 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1afw |
| Chain | Residue | Details |
| A | HIS348 | |
| A | GLY380 | |
| A | CYS378 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1afw |
| Chain | Residue | Details |
| B | HIS348 | |
| B | GLY380 | |
| B | CYS378 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1afw |
| Chain | Residue | Details |
| D | HIS348 | |
| D | GLY380 | |
| D | CYS378 |
| site_id | CSA4 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1afw |
| Chain | Residue | Details |
| C | HIS348 | |
| C | GLY380 | |
| C | CYS378 | |
| C | CYS89 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1afw |
| Chain | Residue | Details |
| A | HIS348 | |
| A | CYS378 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1afw |
| Chain | Residue | Details |
| B | HIS348 | |
| B | CYS378 |
| site_id | CSA7 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1afw |
| Chain | Residue | Details |
| D | HIS348 | |
| D | CYS378 |
| site_id | CSA8 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1afw |
| Chain | Residue | Details |
| C | HIS348 | |
| C | CYS378 |
