2F1F
Crystal structure of the regulatory subunit of acetohydroxyacid synthase isozyme III from E. coli
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003984 | molecular_function | acetolactate synthase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0005948 | cellular_component | acetolactate synthase complex |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0009082 | biological_process | branched-chain amino acid biosynthetic process |
| A | 0009097 | biological_process | isoleucine biosynthetic process |
| A | 0009099 | biological_process | L-valine biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 1990610 | molecular_function | acetolactate synthase regulator activity |
| B | 0003984 | molecular_function | acetolactate synthase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0005948 | cellular_component | acetolactate synthase complex |
| B | 0008652 | biological_process | amino acid biosynthetic process |
| B | 0009082 | biological_process | branched-chain amino acid biosynthetic process |
| B | 0009097 | biological_process | isoleucine biosynthetic process |
| B | 0009099 | biological_process | L-valine biosynthetic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 1990610 | molecular_function | acetolactate synthase regulator activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE MG A 801 |
| Chain | Residue |
| A | HOH803 |
| A | HOH805 |
| A | HOH805 |
| A | HOH805 |
| A | HOH803 |
| A | HOH803 |
| A | HOH803 |
| A | HOH804 |
| A | HOH804 |
| A | HOH804 |
| A | HOH804 |
| A | HOH805 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE MG B 901 |
| Chain | Residue |
| B | HOH903 |
| B | HOH903 |
| B | HOH903 |
| B | HOH903 |
| B | HOH904 |
| B | HOH904 |
| B | HOH904 |
| B | HOH904 |
| B | HOH905 |
| B | HOH905 |
| B | HOH905 |
| B | HOH905 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE MG B 805 |
| Chain | Residue |
| B | MG810 |
| B | MG810 |
| B | MG810 |
| B | MG810 |
| B | HOH906 |
| B | HOH906 |
| B | HOH906 |
| B | HOH906 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG B 810 |
| Chain | Residue |
| B | MG805 |
| B | MG805 |
| B | MG805 |
| B | MG805 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 802 |
| Chain | Residue |
| A | GLU10 |
| A | ILE144 |
| A | VAL145 |
| A | HOH863 |
| A | HOH918 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG B 902 |
| Chain | Residue |
| B | GLU10 |
| B | ASP69 |
| B | ASP140 |
| B | HOH956 |
| site_id | AC7 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE P33 B 501 |
| Chain | Residue |
| A | ARG84 |
| A | ARG109 |
| A | ARG157 |
| A | 1PE601 |
| A | HOH853 |
| B | ILE107 |
| B | PHE108 |
| B | GLN111 |
| B | ILE112 |
| B | ILE113 |
| B | LYS130 |
| B | HOH945 |
| B | HOH1011 |
| B | HOH1019 |
| B | HOH1022 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE 1PE A 601 |
| Chain | Residue |
| A | ILE107 |
| A | ARG109 |
| A | ILE112 |
| A | ILE113 |
| A | LYS130 |
| B | ARG157 |
| B | P33501 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 148 |
| Details | Domain: {"description":"ACT","evidences":[{"source":"PROSITE-ProRule","id":"PRU01007","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
