1M4T
Biosynthetic thiolase, Cys89 butyrylated
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003985 | molecular_function | acetyl-CoA C-acetyltransferase activity |
| A | 0003988 | molecular_function | acetyl-CoA C-acyltransferase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0016740 | molecular_function | transferase activity |
| 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 |
| A | 0044281 | biological_process | small molecule metabolic process |
| B | 0003985 | molecular_function | acetyl-CoA C-acetyltransferase activity |
| B | 0003988 | molecular_function | acetyl-CoA C-acyltransferase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0016740 | molecular_function | transferase activity |
| 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 |
| B | 0044281 | biological_process | small molecule metabolic process |
| C | 0003985 | molecular_function | acetyl-CoA C-acetyltransferase activity |
| C | 0003988 | molecular_function | acetyl-CoA C-acyltransferase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0016740 | molecular_function | transferase activity |
| 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 |
| C | 0044281 | biological_process | small molecule metabolic process |
| D | 0003985 | molecular_function | acetyl-CoA C-acetyltransferase activity |
| D | 0003988 | molecular_function | acetyl-CoA C-acyltransferase activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0016740 | molecular_function | transferase activity |
| 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 |
| D | 0044281 | biological_process | small molecule metabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 A 9720 |
| Chain | Residue |
| A | SER260 |
| A | ARG266 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 9722 |
| Chain | Residue |
| A | LYS298 |
| A | ARG302 |
| A | HOH9943 |
| B | GLY106 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 5394 |
| Chain | Residue |
| A | HOH394 |
| A | HOH477 |
| A | HOH9857 |
| A | HOH9927 |
| A | ALA37 |
| A | ARG41 |
| A | ILE199 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 9719 |
| Chain | Residue |
| A | GLY106 |
| B | LYS298 |
| B | ARG302 |
| B | HOH9865 |
| B | HOH9897 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B 9721 |
| Chain | Residue |
| B | SER260 |
| B | ALA262 |
| B | ARG266 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 6394 |
| Chain | Residue |
| B | GLU40 |
| B | ARG41 |
| B | ILE199 |
| B | VAL200 |
| B | HOH9909 |
| B | HOH9998 |
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 | CY489 | |
| B | CY489 | |
| C | CY489 | |
| D | CY489 |
| 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 |
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 |
| C | HIS348 | |
| C | GLY380 | |
| C | CYS378 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1afw |
| Chain | Residue | Details |
| D | HIS348 | |
| D | GLY380 | |
| D | CYS378 |
| 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 |
| C | HIS348 | |
| C | CYS378 |
| site_id | CSA8 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1afw |
| Chain | Residue | Details |
| D | HIS348 | |
| D | CYS378 |
