5GRF
Crystal structure of the alpha gamma mutant (gamma-K151A) of human IDH3 in complex with Mg(2+), citrate and ADP
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 | 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 | 0045242 | cellular_component | isocitrate dehydrogenase complex (NAD+) |
| 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 | 0001917 | cellular_component | photoreceptor inner segment |
| 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 | 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 | 0045242 | cellular_component | isocitrate dehydrogenase complex (NAD+) |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | binding site for residue CIT B 401 |
| Chain | Residue |
| A | LYS173 |
| B | ASN239 |
| B | ARG272 |
| B | MG403 |
| B | HOH586 |
| A | ASN175 |
| B | ASN78 |
| B | THR81 |
| B | SER91 |
| B | ASN93 |
| B | ARG97 |
| B | ARG128 |
| B | TYR135 |
| site_id | AC2 |
| Number of Residues | 17 |
| Details | binding site for residue ADP B 402 |
| Chain | Residue |
| A | TYR204 |
| A | THR207 |
| B | ILE26 |
| B | PRO252 |
| B | ARG272 |
| B | ASN273 |
| B | THR274 |
| B | GLY275 |
| B | LYS276 |
| B | SER277 |
| B | ILE278 |
| B | ASN285 |
| B | ASP326 |
| B | MG403 |
| B | HOH503 |
| B | HOH532 |
| B | HOH579 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue MG B 403 |
| Chain | Residue |
| B | ASN78 |
| B | ARG272 |
| B | CIT401 |
| B | ADP402 |
| B | HOH579 |
| B | HOH586 |
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 | 14 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"28098230","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Site: {"description":"Critical for catalysis","evidences":[{"source":"PubMed","id":"28098230","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28139779","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Site: {"description":"Critical for catalysis","evidences":[{"source":"PubMed","id":"28098230","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q9D6R2","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9D6R2","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q9D6R2","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q9D6R2","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
