6AQJ
Crystal structures of Staphylococcus aureus ketol-acid reductoisomerase in complex with two transition state analogs that have biocidal activity.
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 | 0005829 | cellular_component | cytosol |
| 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 | 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 | 0005829 | cellular_component | cytosol |
| 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 | 0016491 | molecular_function | oxidoreductase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0050661 | molecular_function | NADP binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | binding site for residue MG A 401 |
| Chain | Residue |
| A | ASP190 |
| A | MG402 |
| A | 40E403 |
| A | HIO408 |
| A | HOH501 |
| A | HOH555 |
| A | HOH595 |
| B | HOH536 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue MG A 402 |
| Chain | Residue |
| A | GLU194 |
| A | MG401 |
| A | 40E403 |
| A | HIO408 |
| A | HOH549 |
| A | HOH668 |
| A | ASP190 |
| site_id | AC3 |
| Number of Residues | 18 |
| Details | binding site for residue 40E A 403 |
| Chain | Residue |
| A | PRO132 |
| A | ASP190 |
| A | GLU194 |
| A | CYS199 |
| A | MG401 |
| A | MG402 |
| A | NDP407 |
| A | HIO408 |
| A | HOH501 |
| A | HOH549 |
| A | HOH555 |
| A | HOH595 |
| A | HOH668 |
| B | GLU230 |
| B | ILE234 |
| B | ILE250 |
| B | SER251 |
| B | ALA254 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue GOL A 404 |
| Chain | Residue |
| A | ARG138 |
| A | THR139 |
| A | GLU142 |
| A | HOH502 |
| B | ASP236 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 405 |
| Chain | Residue |
| A | TYR25 |
| A | GLY26 |
| A | HIS134 |
| A | GOL406 |
| A | HOH509 |
| A | HOH680 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | binding site for residue GOL A 406 |
| Chain | Residue |
| A | GLY26 |
| A | SER27 |
| A | GOL405 |
| A | NDP407 |
| A | HOH507 |
| A | HOH566 |
| A | HOH684 |
| B | TYR248 |
| site_id | AC7 |
| Number of Residues | 42 |
| Details | binding site for residue NDP A 407 |
| Chain | Residue |
| A | TYR25 |
| A | GLY26 |
| A | SER27 |
| A | GLN28 |
| A | ILE47 |
| A | ARG48 |
| A | SER52 |
| A | LEU79 |
| A | LEU80 |
| A | PRO81 |
| A | ASP82 |
| A | ILE84 |
| A | GLN85 |
| A | VAL88 |
| A | ALA106 |
| A | HIS107 |
| A | PRO129 |
| A | GLY131 |
| A | PRO132 |
| A | GLY133 |
| A | 40E403 |
| A | GOL406 |
| A | HIO408 |
| A | HOH514 |
| A | HOH516 |
| A | HOH535 |
| A | HOH542 |
| A | HOH545 |
| A | HOH566 |
| A | HOH584 |
| A | HOH600 |
| A | HOH615 |
| A | HOH623 |
| A | HOH624 |
| A | HOH643 |
| A | HOH668 |
| A | HOH698 |
| A | HOH708 |
| B | SER249 |
| B | ILE250 |
| B | SER251 |
| B | HOH710 |
| site_id | AC8 |
| Number of Residues | 16 |
| Details | binding site for residue HIO A 408 |
| Chain | Residue |
| A | MG402 |
| A | 40E403 |
| A | NDP407 |
| A | HOH501 |
| A | HOH555 |
| A | HOH668 |
| B | GLU230 |
| B | ILE234 |
| B | ILE250 |
| B | SER251 |
| B | ALA254 |
| A | PRO132 |
| A | ASP190 |
| A | GLU194 |
| A | CYS199 |
| A | MG401 |
| site_id | AC9 |
| Number of Residues | 17 |
| Details | binding site for residue 40E B 401 |
| Chain | Residue |
| A | GLU230 |
| A | ILE234 |
| A | ILE250 |
| A | SER251 |
| A | ALA254 |
| B | PRO132 |
| B | ASP190 |
| B | GLU194 |
| B | CYS199 |
| B | HIO402 |
| B | MG403 |
| B | MG404 |
| B | NDP408 |
| B | HOH501 |
| B | HOH543 |
| B | HOH560 |
| B | HOH683 |
| site_id | AD1 |
| Number of Residues | 17 |
| Details | binding site for residue HIO B 402 |
| Chain | Residue |
| A | GLU230 |
| A | ILE250 |
| A | SER251 |
| A | ALA254 |
| B | PRO132 |
| B | ASP190 |
| B | GLU194 |
| B | CYS199 |
| B | 40E401 |
| B | MG403 |
| B | MG404 |
| B | NDP408 |
| B | HOH501 |
| B | HOH543 |
| B | HOH551 |
| B | HOH560 |
| B | HOH683 |
| site_id | AD2 |
| Number of Residues | 7 |
| Details | binding site for residue MG B 403 |
| Chain | Residue |
| A | HOH540 |
| B | ASP190 |
| B | 40E401 |
| B | HIO402 |
| B | HOH501 |
| B | HOH543 |
| B | HOH551 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | binding site for residue MG B 404 |
| Chain | Residue |
| B | ASP190 |
| B | GLU194 |
| B | 40E401 |
| B | HIO402 |
| B | HOH560 |
| B | HOH683 |
| site_id | AD4 |
| Number of Residues | 6 |
| Details | binding site for residue GOL B 405 |
| Chain | Residue |
| A | ASP236 |
| B | ARG138 |
| B | THR139 |
| B | GLU142 |
| B | HOH504 |
| B | HOH570 |
| site_id | AD5 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 406 |
| Chain | Residue |
| B | HIS134 |
| B | HOH509 |
| B | HOH513 |
| B | HOH779 |
| site_id | AD6 |
| Number of Residues | 2 |
| Details | binding site for residue EDO B 407 |
| Chain | Residue |
| B | LYS184 |
| B | HOH510 |
| site_id | AD7 |
| Number of Residues | 38 |
| Details | binding site for residue NDP B 408 |
| Chain | Residue |
| A | SER249 |
| A | ILE250 |
| A | SER251 |
| B | TYR25 |
| B | GLY26 |
| B | SER27 |
| B | GLN28 |
| B | ILE47 |
| B | ARG48 |
| B | SER52 |
| B | LEU79 |
| B | LEU80 |
| B | PRO81 |
| B | ASP82 |
| B | GLN85 |
| B | VAL88 |
| B | ALA106 |
| B | HIS107 |
| B | PRO129 |
| B | GLY131 |
| B | PRO132 |
| B | GLY133 |
| B | 40E401 |
| B | HIO402 |
| B | HOH512 |
| B | HOH538 |
| B | HOH559 |
| B | HOH564 |
| B | HOH610 |
| B | HOH622 |
| B | HOH638 |
| B | HOH646 |
| B | HOH662 |
| B | HOH683 |
| B | HOH685 |
| B | HOH688 |
| B | HOH703 |
| B | HOH741 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 290 |
| Details | Domain: {"description":"KARI C-terminal knotted","evidences":[{"source":"PROSITE-ProRule","id":"PRU01198","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00435","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 28 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00435","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
