6VO2
Crystal structure of Staphylococcus aureus ketol-acid reductoisomerase in complex with Mg, NADPH and inhibitor.
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 | MG402 |
| A | HOH568 |
| A | HOH673 |
| B | R67403 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 402 |
| Chain | Residue |
| A | HOH657 |
| B | R67403 |
| B | HOH542 |
| A | ASP190 |
| A | MG401 |
| A | HOH589 |
| site_id | AC3 |
| Number of Residues | 17 |
| Details | binding site for residue R67 A 403 |
| Chain | Residue |
| A | GLU230 |
| A | ILE234 |
| A | ILE250 |
| A | SER251 |
| A | ALA254 |
| A | HOH539 |
| A | HOH664 |
| B | GLY131 |
| B | PRO132 |
| B | ASP190 |
| B | GLU194 |
| B | MG401 |
| B | MG402 |
| B | NDP404 |
| B | HOH551 |
| B | HOH587 |
| B | HOH628 |
| site_id | AC4 |
| Number of Residues | 36 |
| Details | binding site for residue NDP A 404 |
| 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 | GLN85 |
| A | VAL88 |
| A | ALA106 |
| A | HIS107 |
| A | GLY131 |
| A | PRO132 |
| A | GLY133 |
| A | HOH525 |
| A | HOH555 |
| A | HOH589 |
| A | HOH592 |
| A | HOH609 |
| A | HOH614 |
| A | HOH630 |
| A | HOH633 |
| A | HOH649 |
| A | HOH661 |
| A | HOH673 |
| A | HOH694 |
| A | HOH770 |
| B | SER249 |
| B | ILE250 |
| B | SER251 |
| B | R67403 |
| B | HOH595 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue MG B 401 |
| Chain | Residue |
| A | R67403 |
| A | HOH539 |
| A | HOH664 |
| B | ASP190 |
| B | MG402 |
| B | HOH587 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue MG B 402 |
| Chain | Residue |
| A | R67403 |
| B | ASP190 |
| B | GLU194 |
| B | MG401 |
| B | HOH551 |
| B | HOH628 |
| site_id | AC7 |
| Number of Residues | 16 |
| Details | binding site for residue R67 B 403 |
| Chain | Residue |
| A | GLY131 |
| A | PRO132 |
| A | ASP190 |
| A | GLU194 |
| A | MG401 |
| A | MG402 |
| A | NDP404 |
| A | HOH568 |
| A | HOH589 |
| A | HOH657 |
| A | HOH673 |
| B | GLU230 |
| B | ILE250 |
| B | SER251 |
| B | ALA254 |
| B | HOH542 |
| site_id | AC8 |
| Number of Residues | 39 |
| Details | binding site for residue NDP B 404 |
| Chain | Residue |
| 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 | PRO132 |
| B | GLY133 |
| B | HOH520 |
| B | HOH524 |
| B | HOH525 |
| B | HOH528 |
| B | HOH549 |
| B | HOH552 |
| B | HOH555 |
| B | HOH567 |
| B | HOH575 |
| B | HOH587 |
| B | HOH614 |
| B | HOH628 |
| B | HOH629 |
| B | HOH646 |
| B | HOH655 |
| B | HOH660 |
| B | HOH692 |
| B | HOH714 |
| A | SER249 |
| A | ILE250 |
| A | SER251 |
| A | R67403 |
| B | TYR25 |
| B | GLY26 |
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 |
