5W3K
Crystal structure of Staphylococcus aureus ketol-acid reductoisomerase in complex NADPH, Mg2+ and CPD
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 | 13 |
Details | binding site for residue 9TY A 401 |
Chain | Residue |
A | GLU230 |
B | NDP404 |
B | HOH543 |
B | HOH565 |
B | HOH690 |
A | ILE250 |
A | SER251 |
A | ALA254 |
A | HOH568 |
B | ASP190 |
B | GLU194 |
B | MG402 |
B | MG403 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue MG A 402 |
Chain | Residue |
A | ASP190 |
A | HOH574 |
B | 9TY401 |
B | HOH537 |
B | HOH559 |
site_id | AC3 |
Number of Residues | 5 |
Details | binding site for residue MG A 403 |
Chain | Residue |
A | ASP190 |
A | GLU194 |
A | HOH531 |
A | HOH664 |
B | 9TY401 |
site_id | AC4 |
Number of Residues | 6 |
Details | binding site for residue MG A 404 |
Chain | Residue |
A | VAL70 |
A | LYS71 |
A | ALA73 |
A | ASN101 |
A | HOH543 |
A | HOH654 |
site_id | AC5 |
Number of Residues | 2 |
Details | binding site for residue MG A 405 |
Chain | Residue |
A | ASN39 |
A | HOH781 |
site_id | AC6 |
Number of Residues | 36 |
Details | binding site for residue NDP A 406 |
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 | HOH501 |
A | HOH506 |
A | HOH513 |
A | HOH518 |
A | HOH520 |
A | HOH533 |
A | HOH547 |
A | HOH556 |
A | HOH557 |
A | HOH600 |
A | HOH605 |
A | HOH664 |
B | SER249 |
B | ILE250 |
B | SER251 |
B | 9TY401 |
site_id | AC7 |
Number of Residues | 13 |
Details | binding site for residue 9TY B 401 |
Chain | Residue |
A | ASP190 |
A | GLU194 |
A | MG402 |
A | MG403 |
A | NDP406 |
A | HOH531 |
A | HOH574 |
A | HOH664 |
B | GLU230 |
B | ILE250 |
B | SER251 |
B | ALA254 |
B | HOH559 |
site_id | AC8 |
Number of Residues | 6 |
Details | binding site for residue MG B 402 |
Chain | Residue |
A | 9TY401 |
A | HOH519 |
A | HOH568 |
B | ASP190 |
B | MG403 |
B | HOH565 |
site_id | AC9 |
Number of Residues | 6 |
Details | binding site for residue MG B 403 |
Chain | Residue |
A | 9TY401 |
B | ASP190 |
B | GLU194 |
B | MG402 |
B | HOH543 |
B | HOH690 |
site_id | AD1 |
Number of Residues | 41 |
Details | binding site for residue NDP B 404 |
Chain | Residue |
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 | HOH509 |
B | HOH510 |
B | HOH514 |
B | HOH532 |
B | HOH544 |
B | HOH545 |
B | HOH591 |
B | HOH594 |
B | HOH617 |
B | HOH624 |
B | HOH632 |
B | HOH654 |
B | HOH670 |
B | HOH675 |
B | HOH684 |
B | HOH685 |
B | HOH690 |
B | HOH728 |
A | SER249 |
A | ILE250 |
A | SER251 |
A | 9TY401 |
B | TYR25 |
B | GLY26 |
B | SER27 |
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 |