1A05
CRYSTAL STRUCTURE OF THE COMPLEX OF 3-ISOPROPYLMALATE DEHYDROGENASE FROM THIOBACILLUS FERROOXIDANS WITH 3-ISOPROPYLMALATE
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 | 0005829 | cellular_component | cytosol |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0009082 | biological_process | branched-chain amino acid biosynthetic process |
| 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 | 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 | 0005829 | cellular_component | cytosol |
| B | 0008652 | biological_process | amino acid biosynthetic process |
| B | 0009082 | biological_process | branched-chain amino acid biosynthetic process |
| 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 | 0046872 | molecular_function | metal ion binding |
| B | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 501 |
| Chain | Residue |
| A | ASP246 |
| A | IPM401 |
| A | HOH562 |
| A | HOH602 |
| B | ASP222 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 502 |
| Chain | Residue |
| B | HOH419 |
| A | ASP222 |
| A | HOH532 |
| B | ASP246 |
| B | IPM402 |
| site_id | AC3 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE IPM A 401 |
| Chain | Residue |
| A | GLU88 |
| A | ARG95 |
| A | ARG105 |
| A | ARG133 |
| A | TYR140 |
| A | ASP246 |
| A | MG501 |
| A | HOH553 |
| A | HOH693 |
| B | LYS190 |
| B | VAL193 |
| B | ASP222 |
| site_id | AC4 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE IPM B 402 |
| Chain | Residue |
| A | LYS190 |
| A | VAL193 |
| A | ASP222 |
| A | MG502 |
| B | ARG95 |
| B | ARG105 |
| B | ARG133 |
| B | TYR140 |
| B | ASP246 |
| B | HOH428 |
| B | HOH441 |
Functional Information from PROSITE/UniProt
| site_id | PS00470 |
| Number of Residues | 20 |
| Details | IDH_IMDH Isocitrate and isopropylmalate dehydrogenases signature. NMFGDIlSDeaSqlt.GSIGM |
| Chain | Residue | Details |
| A | ASN242-MET261 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01033 |
| Chain | Residue | Details |
| B | ASP250 | |
| B | GLY279 | |
| A | GLY75 | |
| A | ASP250 | |
| A | GLY279 | |
| B | GLY75 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01033, ECO:0000269|PubMed:9739088 |
| Chain | Residue | Details |
| B | ARG95 | |
| B | ARG105 | |
| B | ARG133 | |
| B | ASP222 | |
| A | ARG95 | |
| A | ARG105 | |
| A | ARG133 | |
| A | ASP222 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:9739088, ECO:0007744|PDB:1A05 |
| Chain | Residue | Details |
| A | ASP246 | |
| B | ASP246 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | SITE: Important for catalysis => ECO:0000255|HAMAP-Rule:MF_01033, ECO:0000305|PubMed:9739088 |
| Chain | Residue | Details |
| A | TYR140 | |
| A | LYS190 | |
| B | TYR140 | |
| B | LYS190 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 371 |
| Chain | Residue | Details |
| A | TYR140 | electron shuttle |
| A | LYS190 | proton shuttle (general acid/base) |
| A | ASP222 | metal ligand, proton shuttle (general acid/base) |
| A | ASP246 | metal ligand |
| A | ASP250 | metal ligand |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 371 |
| Chain | Residue | Details |
| B | TYR140 | electron shuttle |
| B | LYS190 | proton shuttle (general acid/base) |
| B | ASP222 | metal ligand, proton shuttle (general acid/base) |
| B | ASP246 | metal ligand |
| B | ASP250 | metal ligand |
