4XIY
Crystal structure of ketol-acid reductoisomerase from Azotobacter
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 |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0004455 | molecular_function | ketol-acid reductoisomerase activity |
| C | 0005829 | cellular_component | cytosol |
| C | 0008652 | biological_process | amino acid biosynthetic process |
| C | 0009082 | biological_process | branched-chain amino acid biosynthetic process |
| C | 0009097 | biological_process | isoleucine biosynthetic process |
| C | 0009099 | biological_process | L-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 | 0005829 | cellular_component | cytosol |
| D | 0008652 | biological_process | amino acid biosynthetic process |
| D | 0009082 | biological_process | branched-chain amino acid biosynthetic process |
| D | 0009097 | biological_process | isoleucine biosynthetic process |
| D | 0009099 | biological_process | L-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 | 5 |
| Details | binding site for residue MG A 401 |
| Chain | Residue |
| A | GLU226 |
| A | GLU230 |
| B | ASP190 |
| B | HOH506 |
| B | HOH507 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | binding site for residue FE A 402 |
| Chain | Residue |
| A | ASP190 |
| A | GLU194 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue PGE A 403 |
| Chain | Residue |
| A | ARG305 |
| A | TYR298 |
| A | THR302 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue MG B 401 |
| Chain | Residue |
| A | ASP190 |
| B | GLU226 |
| B | GLU230 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue FE B 402 |
| Chain | Residue |
| B | ASP190 |
| B | GLU194 |
| B | HOH501 |
| B | HOH503 |
| B | HOH504 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue PGE B 403 |
| Chain | Residue |
| A | ASN252 |
| B | TYR298 |
| B | THR302 |
| B | ARG305 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | binding site for residue FE C 401 |
| Chain | Residue |
| C | ASP190 |
| C | GLU194 |
| C | HOH501 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue MG C 402 |
| Chain | Residue |
| C | GLU226 |
| C | GLU230 |
| C | HOH506 |
| D | ASP190 |
| D | HOH509 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | binding site for residue PEG C 403 |
| Chain | Residue |
| C | TYR298 |
| C | THR302 |
| C | ARG305 |
| site_id | AD1 |
| Number of Residues | 3 |
| Details | binding site for residue MG D 401 |
| Chain | Residue |
| C | ASP190 |
| D | GLU226 |
| D | GLU230 |
| site_id | AD2 |
| Number of Residues | 6 |
| Details | binding site for residue FE D 402 |
| Chain | Residue |
| C | HOH505 |
| D | ASP190 |
| D | GLU194 |
| D | HOH502 |
| D | HOH503 |
| D | HOH508 |
| site_id | AD3 |
| Number of Residues | 4 |
| Details | binding site for residue PG4 D 403 |
| Chain | Residue |
| C | TYR248 |
| D | TYR298 |
| D | THR302 |
| D | ARG305 |
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 | HIS107 | |
| B | HIS107 | |
| C | HIS107 | |
| D | HIS107 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 28 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00435 |
| Chain | Residue | Details |
| A | TYR24 | |
| B | SER50 | |
| B | SER52 | |
| B | ASP82 | |
| B | GLY133 | |
| B | SER251 | |
| C | TYR24 | |
| C | ARG47 | |
| C | SER50 | |
| C | SER52 | |
| C | ASP82 | |
| A | ARG47 | |
| C | GLY133 | |
| C | SER251 | |
| D | TYR24 | |
| D | ARG47 | |
| D | SER50 | |
| D | SER52 | |
| D | ASP82 | |
| D | GLY133 | |
| D | SER251 | |
| A | SER50 | |
| A | SER52 | |
| A | ASP82 | |
| A | GLY133 | |
| A | SER251 | |
| B | TYR24 | |
| B | ARG47 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00435, ECO:0000269|PubMed:25849365 |
| Chain | Residue | Details |
| A | ASP190 | |
| D | ASP190 | |
| D | GLU226 | |
| D | GLU230 | |
| A | GLU226 | |
| A | GLU230 | |
| B | ASP190 | |
| B | GLU226 | |
| B | GLU230 | |
| C | ASP190 | |
| C | GLU226 | |
| C | GLU230 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00435, ECO:0000305|PubMed:25849365 |
| Chain | Residue | Details |
| A | GLU194 | |
| B | GLU194 | |
| C | GLU194 | |
| D | GLU194 |
