3FR8
rice Ketolacid reductoisomerase in complex with Mg2+-NADPH
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 | 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 | 0009507 | cellular_component | chloroplast |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0070402 | molecular_function | NADPH binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0004455 | molecular_function | ketol-acid reductoisomerase activity |
| 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 | 0009507 | cellular_component | chloroplast |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0070402 | molecular_function | NADPH binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 1 |
| Chain | Residue |
| A | ASP315 |
| A | GLU492 |
| A | GLU496 |
| A | HOH663 |
| A | PE46061 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 597 |
| Chain | Residue |
| A | PHE463 |
| A | ARG337 |
| A | TYR338 |
| A | GLN341 |
| A | HIS461 |
| site_id | AC3 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE NDP A 601 |
| Chain | Residue |
| A | TRP133 |
| A | GLY134 |
| A | SER135 |
| A | GLN136 |
| A | ARG162 |
| A | SER165 |
| A | SER167 |
| A | LEU199 |
| A | ILE200 |
| A | SER201 |
| A | ASP202 |
| A | ALA204 |
| A | GLN205 |
| A | ASN208 |
| A | SER225 |
| A | HIS226 |
| A | GLY253 |
| A | MET254 |
| A | SER518 |
| A | PE46061 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PE4 A6061 |
| Chain | Residue |
| A | MG1 |
| A | ASP315 |
| A | GLU319 |
| A | GLU496 |
| A | CYS517 |
| A | SER518 |
| A | NDP601 |
| A | HOH663 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 1 |
| Chain | Residue |
| B | HIS226 |
| B | ASP315 |
| B | GLU319 |
| B | HOH667 |
| B | PEG6073 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG B 597 |
| Chain | Residue |
| B | ASP315 |
| B | GLU496 |
| B | HOH670 |
| B | PEG6073 |
| site_id | AC7 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE NDP B 600 |
| Chain | Residue |
| B | TRP133 |
| B | GLY134 |
| B | SER135 |
| B | GLN136 |
| B | ARG162 |
| B | SER165 |
| B | SER167 |
| B | LEU199 |
| B | ILE200 |
| B | SER201 |
| B | ASP202 |
| B | ALA204 |
| B | GLN205 |
| B | ASN208 |
| B | SER225 |
| B | HIS226 |
| B | PRO251 |
| B | GLY253 |
| B | MET254 |
| B | GLY255 |
| B | SER518 |
| B | THR519 |
| B | ARG589 |
| B | PEG6073 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PEG B6073 |
| Chain | Residue |
| B | MG1 |
| B | ASP315 |
| B | GLU319 |
| B | GLU496 |
| B | SER518 |
| B | MG597 |
| B | NDP600 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 396 |
| Details | Domain: {"description":"KARI N-terminal Rossmann","evidences":[{"source":"PROSITE-ProRule","id":"PRU01197","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 296 |
| Details | Domain: {"description":"KARI C-terminal knotted 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU01198","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Active site: {"evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 32 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"19362563","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01198","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 136 |
| Details | Domain: {"description":"KARI C-terminal knotted 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU01198","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1yve |
| Chain | Residue | Details |
| A | GLU496 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1yve |
| Chain | Residue | Details |
| B | GLU496 |
