6JX2
Crystal structure of Ketol-acid reductoisomerase from Corynebacterium glutamicum
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0004455 | molecular_function | ketol-acid reductoisomerase activity |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0008677 | molecular_function | 2-dehydropantoate 2-reductase activity |
| A | 0009082 | biological_process | branched-chain amino acid biosynthetic process |
| A | 0009097 | biological_process | isoleucine biosynthetic process |
| A | 0009099 | biological_process | valine biosynthetic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050661 | molecular_function | NADP binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0004455 | molecular_function | ketol-acid reductoisomerase activity |
| B | 0008652 | biological_process | amino acid biosynthetic process |
| B | 0008677 | molecular_function | 2-dehydropantoate 2-reductase activity |
| B | 0009082 | biological_process | branched-chain amino acid biosynthetic process |
| B | 0009097 | biological_process | isoleucine biosynthetic process |
| B | 0009099 | biological_process | valine biosynthetic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0050661 | molecular_function | NADP binding |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0004455 | molecular_function | ketol-acid reductoisomerase activity |
| C | 0008652 | biological_process | amino acid biosynthetic process |
| C | 0008677 | molecular_function | 2-dehydropantoate 2-reductase activity |
| C | 0009082 | biological_process | branched-chain amino acid biosynthetic process |
| C | 0009097 | biological_process | isoleucine biosynthetic process |
| C | 0009099 | biological_process | valine biosynthetic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0050661 | molecular_function | NADP binding |
| D | 0000287 | molecular_function | magnesium ion binding |
| D | 0004455 | molecular_function | ketol-acid reductoisomerase activity |
| D | 0008652 | biological_process | amino acid biosynthetic process |
| D | 0008677 | molecular_function | 2-dehydropantoate 2-reductase activity |
| D | 0009082 | biological_process | branched-chain amino acid biosynthetic process |
| D | 0009097 | biological_process | isoleucine biosynthetic process |
| D | 0009099 | biological_process | valine biosynthetic process |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0050661 | molecular_function | NADP binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 2 |
| Details | binding site for residue MG A 401 |
| Chain | Residue |
| A | ASP192 |
| A | GLU196 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue MG A 402 |
| Chain | Residue |
| A | GLU228 |
| A | GLU232 |
| B | ASP192 |
| B | GLU196 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue MG A 403 |
| Chain | Residue |
| A | ASN100 |
| A | ASP103 |
| A | ALA73 |
| A | ALA75 |
| A | ASN98 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | binding site for residue MG A 404 |
| Chain | Residue |
| A | TYR250 |
| A | ASP254 |
| site_id | AC5 |
| Number of Residues | 15 |
| Details | binding site for residue NAP A 405 |
| Chain | Residue |
| A | GLY25 |
| A | TYR26 |
| A | GLY27 |
| A | SER28 |
| A | ARG49 |
| A | SER52 |
| A | LYS53 |
| A | SER54 |
| A | THR68 |
| A | LEU81 |
| A | ALA82 |
| A | PRO83 |
| A | ILE90 |
| A | HOH509 |
| A | HOH533 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | binding site for residue EDO A 406 |
| Chain | Residue |
| A | GLU297 |
| A | HOH514 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 407 |
| Chain | Residue |
| A | ASP116 |
| A | ASP155 |
| A | GLN156 |
| A | HOH518 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | binding site for residue MG B 401 |
| Chain | Residue |
| A | ASP192 |
| B | GLU228 |
| B | GLU232 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | binding site for residue MG B 402 |
| Chain | Residue |
| B | ASP192 |
| B | GLU196 |
| site_id | AD1 |
| Number of Residues | 1 |
| Details | binding site for residue MG B 403 |
| Chain | Residue |
| B | ASP116 |
| site_id | AD2 |
| Number of Residues | 1 |
| Details | binding site for residue MG B 404 |
| Chain | Residue |
| B | ASP254 |
| site_id | AD3 |
| Number of Residues | 4 |
| Details | binding site for residue MG B 405 |
| Chain | Residue |
| B | ALA73 |
| B | ALA75 |
| B | ASN100 |
| B | ASP103 |
| site_id | AD4 |
| Number of Residues | 2 |
| Details | binding site for residue EDO B 406 |
| Chain | Residue |
| B | ASP123 |
| B | GLU213 |
| site_id | AD5 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 407 |
| Chain | Residue |
| B | GLU4 |
| B | LEU5 |
| D | ASP10 |
| D | ASN298 |
| site_id | AD6 |
| Number of Residues | 3 |
| Details | binding site for residue EDO B 408 |
| Chain | Residue |
| B | HIS114 |
| B | THR184 |
| B | GLU186 |
| site_id | AD7 |
| Number of Residues | 2 |
| Details | binding site for residue MG C 401 |
| Chain | Residue |
| C | ASP192 |
| C | GLU196 |
| site_id | AD8 |
| Number of Residues | 3 |
| Details | binding site for residue MG C 402 |
| Chain | Residue |
| C | GLU228 |
| C | GLU232 |
| D | ASP192 |
| site_id | AD9 |
| Number of Residues | 19 |
| Details | binding site for residue NAP C 403 |
| Chain | Residue |
| C | GLY25 |
| C | TYR26 |
| C | GLY27 |
| C | SER28 |
| C | GLN29 |
| C | SER52 |
| C | SER54 |
| C | THR68 |
| C | LEU81 |
| C | ALA82 |
| C | PRO83 |
| C | ASP84 |
| C | GLN87 |
| C | ILE90 |
| C | GLY108 |
| C | HIS109 |
| C | GLY133 |
| C | PRO134 |
| C | HOH501 |
| site_id | AE1 |
| Number of Residues | 4 |
| Details | binding site for residue MG D 401 |
| Chain | Residue |
| C | ASP192 |
| C | GLU196 |
| D | GLU228 |
| D | GLU232 |
| site_id | AE2 |
| Number of Residues | 2 |
| Details | binding site for residue MG D 402 |
| Chain | Residue |
| D | ASP192 |
| D | GLU196 |
| site_id | AE3 |
| Number of Residues | 12 |
| Details | binding site for residue NAP D 403 |
| Chain | Residue |
| D | GLY25 |
| D | TYR26 |
| D | GLY27 |
| D | SER28 |
| D | ARG49 |
| D | SER52 |
| D | LYS53 |
| D | SER54 |
| D | THR68 |
| D | LEU81 |
| D | PRO83 |
| D | ILE90 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00435 |
| Chain | Residue | Details |
| A | HIS109 | |
| B | HIS109 | |
| C | HIS109 | |
| D | HIS109 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 44 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00435 |
| Chain | Residue | Details |
| A | TYR26 | |
| A | GLU232 | |
| A | SER253 | |
| B | TYR26 | |
| B | ARG49 | |
| B | SER52 | |
| B | SER54 | |
| B | ASP84 | |
| B | GLY135 | |
| B | ASP192 | |
| B | GLU196 | |
| A | ARG49 | |
| B | GLU228 | |
| B | GLU232 | |
| B | SER253 | |
| C | TYR26 | |
| C | ARG49 | |
| C | SER52 | |
| C | SER54 | |
| C | ASP84 | |
| C | GLY135 | |
| C | ASP192 | |
| A | SER52 | |
| C | GLU196 | |
| C | GLU228 | |
| C | GLU232 | |
| C | SER253 | |
| D | TYR26 | |
| D | ARG49 | |
| D | SER52 | |
| D | SER54 | |
| D | ASP84 | |
| D | GLY135 | |
| A | SER54 | |
| D | ASP192 | |
| D | GLU196 | |
| D | GLU228 | |
| D | GLU232 | |
| D | SER253 | |
| A | ASP84 | |
| A | GLY135 | |
| A | ASP192 | |
| A | GLU196 | |
| A | GLU228 |
