5SVN
Structure of IDH2 mutant R172K
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0004450 | molecular_function | isocitrate dehydrogenase (NADP+) activity |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005759 | cellular_component | mitochondrial matrix |
| A | 0005777 | cellular_component | peroxisome |
| A | 0005829 | cellular_component | cytosol |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0006097 | biological_process | glyoxylate cycle |
| A | 0006099 | biological_process | tricarboxylic acid cycle |
| A | 0006102 | biological_process | isocitrate metabolic process |
| A | 0006103 | biological_process | 2-oxoglutarate metabolic process |
| A | 0006739 | biological_process | NADP+ metabolic process |
| A | 0006741 | biological_process | NADP+ 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 |
| A | 0060253 | biological_process | negative regulation of glial cell proliferation |
| A | 0070062 | cellular_component | extracellular exosome |
| A | 1903976 | biological_process | negative regulation of glial cell migration |
| A | 1904465 | biological_process | negative regulation of matrix metallopeptidase secretion |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0004450 | molecular_function | isocitrate dehydrogenase (NADP+) activity |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005759 | cellular_component | mitochondrial matrix |
| B | 0005777 | cellular_component | peroxisome |
| B | 0005829 | cellular_component | cytosol |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0006097 | biological_process | glyoxylate cycle |
| B | 0006099 | biological_process | tricarboxylic acid cycle |
| B | 0006102 | biological_process | isocitrate metabolic process |
| B | 0006103 | biological_process | 2-oxoglutarate metabolic process |
| B | 0006739 | biological_process | NADP+ metabolic process |
| B | 0006741 | biological_process | NADP+ 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 |
| B | 0060253 | biological_process | negative regulation of glial cell proliferation |
| B | 0070062 | cellular_component | extracellular exosome |
| B | 1903976 | biological_process | negative regulation of glial cell migration |
| B | 1904465 | biological_process | negative regulation of matrix metallopeptidase secretion |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 30 |
| Details | binding site for residue NDP A 501 |
| Chain | Residue |
| A | LYS112 |
| A | THR350 |
| A | VAL351 |
| A | THR352 |
| A | HIS354 |
| A | ASN367 |
| A | ASP414 |
| A | HOH603 |
| A | HOH612 |
| A | HOH617 |
| A | HOH623 |
| A | ALA114 |
| A | HOH641 |
| A | HOH650 |
| A | HOH660 |
| A | HOH667 |
| A | HOH675 |
| A | HOH682 |
| B | LEU289 |
| B | ASP292 |
| B | GLN296 |
| B | LYS299 |
| A | THR115 |
| B | HOH667 |
| A | ILE116 |
| A | THR117 |
| A | ARG122 |
| A | ASN136 |
| A | HIS348 |
| A | GLY349 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue PEG A 502 |
| Chain | Residue |
| A | PRO245 |
| A | TYR247 |
| A | GLY303 |
| A | HOH604 |
| A | HOH626 |
| site_id | AC3 |
| Number of Residues | 29 |
| Details | binding site for residue NDP B 501 |
| Chain | Residue |
| A | LEU289 |
| A | ASP292 |
| A | GLN296 |
| A | LYS299 |
| A | HOH653 |
| A | HOH665 |
| B | LYS112 |
| B | ALA114 |
| B | THR115 |
| B | ILE116 |
| B | THR117 |
| B | ARG122 |
| B | ASN136 |
| B | HIS348 |
| B | GLY349 |
| B | THR350 |
| B | VAL351 |
| B | THR352 |
| B | HIS354 |
| B | THR366 |
| B | ASN367 |
| B | HOH603 |
| B | HOH624 |
| B | HOH625 |
| B | HOH631 |
| B | HOH639 |
| B | HOH641 |
| B | HOH651 |
| B | HOH669 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | binding site for residue PEG B 502 |
| Chain | Residue |
| B | TYR247 |
| B | GLY302 |
Functional Information from PROSITE/UniProt
| site_id | PS00470 |
| Number of Residues | 20 |
| Details | IDH_IMDH Isocitrate and isopropylmalate dehydrogenases signature. NYDGDVqSDilAqgf.GSLGL |
| Chain | Residue | Details |
| A | ASN310-LEU329 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 20 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"O75874","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 22 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P33198","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Site: {"description":"Critical for catalysis","evidences":[{"source":"UniProtKB","id":"P33198","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 12 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P54071","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 12 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 16 |
| Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P54071","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"22416140","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
