1NP3
Crystal structure of class I acetohydroxy acid isomeroreductase from Pseudomonas aeruginosa
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 | 0009082 | biological_process | branched-chain amino acid biosynthetic process |
| A | 0009099 | biological_process | L-valine biosynthetic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| 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 | 0009082 | biological_process | branched-chain amino acid biosynthetic process |
| B | 0009099 | biological_process | L-valine biosynthetic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| 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 | 0009082 | biological_process | branched-chain amino acid biosynthetic process |
| C | 0009099 | biological_process | L-valine biosynthetic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| 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 | 0009082 | biological_process | branched-chain amino acid biosynthetic process |
| D | 0009099 | biological_process | L-valine biosynthetic process |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0050661 | molecular_function | NADP binding |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 720 |
| Details | Domain: {"description":"KARI N-terminal Rossmann","evidences":[{"source":"PROSITE-ProRule","id":"PRU01197","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12691757","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 580 |
| Details | Domain: {"description":"KARI C-terminal knotted","evidences":[{"source":"PROSITE-ProRule","id":"PRU01198","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12691757","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Active site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00435","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 60 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00435","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 | GLU230 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1yve |
| Chain | Residue | Details |
| B | GLU230 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1yve |
| Chain | Residue | Details |
| C | GLU230 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1yve |
| Chain | Residue | Details |
| D | GLU230 |
