5GRH
Crystal structure of the alpha gamma heterodimer of human IDH3 in complex with Mg(2+)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0004449 | molecular_function | isocitrate dehydrogenase (NAD+) activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005759 | cellular_component | mitochondrial matrix |
| A | 0005962 | cellular_component | obsolete mitochondrial isocitrate dehydrogenase complex (NAD+) |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0006099 | biological_process | tricarboxylic acid cycle |
| A | 0006102 | biological_process | isocitrate metabolic 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 | 0000166 | molecular_function | nucleotide binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0004449 | molecular_function | isocitrate dehydrogenase (NAD+) activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005730 | cellular_component | nucleolus |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005759 | cellular_component | mitochondrial matrix |
| B | 0005962 | cellular_component | obsolete mitochondrial isocitrate dehydrogenase complex (NAD+) |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0006099 | biological_process | tricarboxylic acid cycle |
| B | 0006102 | biological_process | isocitrate metabolic process |
| 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 | 3 |
| Details | binding site for residue MG A 401 |
| Chain | Residue |
| A | ASP230 |
| A | ASP234 |
| B | ASP215 |
Functional Information from PROSITE/UniProt
| site_id | PS00470 |
| Number of Residues | 20 |
| Details | IDH_IMDH Isocitrate and isopropylmalate dehydrogenases signature. NLYGDIlSDlcAgli.GGLGV |
| Chain | Residue | Details |
| A | ASN226-VAL245 | |
| B | ASN235-LEU254 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:28098230 |
| Chain | Residue | Details |
| B | THR81 | |
| B | ASN94 | |
| B | ARG97 | |
| B | ARG128 | |
| B | ASP215 | |
| B | ASN273 | |
| B | THR274 | |
| B | ASN285 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | SITE: Critical for catalysis => ECO:0000269|PubMed:28098230, ECO:0000269|PubMed:28139779 |
| Chain | Residue | Details |
| A | TYR126 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | SITE: Critical for catalysis => ECO:0000269|PubMed:28098230 |
| Chain | Residue | Details |
| A | LYS173 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q9D6R2 |
| Chain | Residue | Details |
| A | LYS50 | |
| A | LYS323 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q9D6R2 |
| Chain | Residue | Details |
| A | THR74 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q9D6R2 |
| Chain | Residue | Details |
| A | LYS196 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9D6R2 |
| Chain | Residue | Details |
| A | LYS316 |
