6C55
Crystal structure of Staphylococcus aureus Ketol-acid Reductosimerrase with hydroxyoxamate inhibitor 3
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 | 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 | 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 | 6 |
| Details | binding site for residue MG A 401 |
| Chain | Residue |
| A | ASP190 |
| A | GLU194 |
| A | EKD404 |
| A | EKA407 |
| A | HOH544 |
| A | HOH602 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | binding site for residue MG A 402 |
| Chain | Residue |
| A | HOH503 |
| A | HOH510 |
| A | HOH518 |
| A | HOH617 |
| B | GLU230 |
| A | ASP190 |
| A | EKD404 |
| A | EKA407 |
| site_id | AC3 |
| Number of Residues | 32 |
| Details | binding site for residue NAP A 403 |
| 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 | ALA106 |
| A | HIS107 |
| A | PRO129 |
| A | GLY131 |
| A | PRO132 |
| A | GLY133 |
| A | EKD404 |
| A | EKA407 |
| A | HOH531 |
| A | HOH533 |
| A | HOH537 |
| A | HOH558 |
| A | HOH569 |
| A | HOH574 |
| A | HOH602 |
| B | SER249 |
| B | ILE250 |
| B | SER251 |
| B | HOH571 |
| site_id | AC4 |
| Number of Residues | 15 |
| Details | binding site for residue EKD A 404 |
| Chain | Residue |
| A | PRO132 |
| A | ASP190 |
| A | GLU194 |
| A | CYS199 |
| A | MG401 |
| A | MG402 |
| A | NAP403 |
| A | EKA407 |
| A | HOH518 |
| A | HOH544 |
| A | HOH602 |
| A | HOH617 |
| B | GLU230 |
| B | SER251 |
| B | ALA254 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | binding site for residue MG A 405 |
| Chain | Residue |
| A | GLU226 |
| A | GLU230 |
| A | EKD406 |
| A | HOH502 |
| A | HOH507 |
| A | HOH628 |
| B | ASP190 |
| B | HOH526 |
| site_id | AC6 |
| Number of Residues | 11 |
| Details | binding site for residue EKD A 406 |
| Chain | Residue |
| A | ILE250 |
| A | SER251 |
| A | ALA254 |
| A | MG405 |
| A | HOH507 |
| A | HOH591 |
| B | ASP190 |
| B | GLU194 |
| B | MG401 |
| B | NAP402 |
| B | HOH522 |
| site_id | AC7 |
| Number of Residues | 17 |
| Details | binding site for residue EKA A 407 |
| Chain | Residue |
| A | PRO132 |
| A | ASP190 |
| A | GLU194 |
| A | CYS199 |
| A | MG401 |
| A | MG402 |
| A | NAP403 |
| A | EKD404 |
| A | HOH503 |
| A | HOH518 |
| A | HOH544 |
| A | HOH602 |
| A | HOH617 |
| B | GLU230 |
| B | ILE250 |
| B | SER251 |
| B | ALA254 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue MG B 401 |
| Chain | Residue |
| B | ASP190 |
| B | GLU194 |
| B | HOH522 |
| A | EKD406 |
| A | HOH591 |
| site_id | AC9 |
| Number of Residues | 28 |
| Details | binding site for residue NAP B 402 |
| Chain | Residue |
| A | SER249 |
| A | ILE250 |
| A | SER251 |
| A | EKD406 |
| A | HOH629 |
| 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 | ALA106 |
| B | HIS107 |
| B | GLY131 |
| B | PRO132 |
| B | GLY133 |
| B | HOH504 |
| B | HOH515 |
| B | HOH551 |
| B | HOH559 |
| B | HOH562 |
| B | HOH570 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00435 |
| Chain | Residue | Details |
| A | HIS107 | |
| B | HIS107 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 20 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00435 |
| Chain | Residue | Details |
| A | TYR25 | |
| A | SER251 | |
| B | TYR25 | |
| B | ARG48 | |
| B | SER52 | |
| B | ASP82 | |
| B | GLY133 | |
| B | ASP190 | |
| B | GLU194 | |
| B | GLU226 | |
| B | GLU230 | |
| A | ARG48 | |
| B | SER251 | |
| A | SER52 | |
| A | ASP82 | |
| A | GLY133 | |
| A | ASP190 | |
| A | GLU194 | |
| A | GLU226 | |
| A | GLU230 |
