1GC8
THE CRYSTAL STRUCTURE OF THERMUS THERMOPHILUS 3-ISOPROPYLMALATE DEHYDROGENASE MUTATED AT 172TH FROM ALA TO PHE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0003862 | molecular_function | 3-isopropylmalate dehydrogenase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0009098 | biological_process | L-leucine biosynthetic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051287 | molecular_function | NAD binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0003862 | molecular_function | 3-isopropylmalate dehydrogenase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0009098 | biological_process | L-leucine biosynthetic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051287 | molecular_function | NAD binding |
Functional Information from PROSITE/UniProt
| site_id | PS00470 |
| Number of Residues | 20 |
| Details | IDH_IMDH Isocitrate and isopropylmalate dehydrogenases signature. NIFGDIlSDlaSvlp.GSLGL |
| Chain | Residue | Details |
| A | ASN1237-LEU1256 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:7881901 |
| Chain | Residue | Details |
| A | GLY1074 | |
| A | GLY1274 | |
| B | GLY74 | |
| B | GLY274 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | ARG1094 | |
| B | ASP217 | |
| B | ASP241 | |
| B | ASP245 | |
| A | ARG1104 | |
| A | ARG1132 | |
| A | ASP1217 | |
| A | ASP1241 | |
| A | ASP1245 | |
| B | ARG94 | |
| B | ARG104 | |
| B | ARG132 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | SITE: Important for catalysis |
| Chain | Residue | Details |
| A | TYR1139 | |
| B | TYR139 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | SITE: Important for catalysis => ECO:0000250 |
| Chain | Residue | Details |
| A | LYS1185 | |
| B | LYS185 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1a05 |
| Chain | Residue | Details |
| A | ASP1217 | |
| A | LYS1185 | |
| B | TYR139 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1a05 |
| Chain | Residue | Details |
| A | TYR1139 | |
| B | LYS185 | |
| B | ASP217 |
