5I96
Crystal Structure of Human Mitochondrial Isocitrate Dehydrogenase (IDH2) R140Q Mutant Homodimer in Complex with AG-221 (Enasidenib) Inhibitor.
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 | 7 |
| Details | binding site for residue CA A 501 |
| Chain | Residue |
| A | ASP314 |
| A | SER317 |
| A | HOH603 |
| A | HOH605 |
| A | HOH830 |
| A | HOH932 |
| B | ASP291 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | binding site for residue GOL A 502 |
| Chain | Residue |
| A | GLU404 |
| A | ASN444 |
| A | HOH612 |
| A | HOH644 |
| A | HOH785 |
| A | HOH814 |
| A | LYS280 |
| A | LYS282 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | binding site for residue GOL A 503 |
| Chain | Residue |
| A | ASP271 |
| A | LYS272 |
| A | HIS273 |
| A | TYR274 |
| A | LYS275 |
| A | THR276 |
| A | HOH786 |
| A | HOH867 |
| A | HOH912 |
| A | HOH1022 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | binding site for residue GOL A 504 |
| Chain | Residue |
| A | PHE184 |
| A | VAL185 |
| A | ALA186 |
| A | ASP187 |
| A | ARG188 |
| A | HOH760 |
| B | TRP207 |
| B | HOH616 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | binding site for residue GOL A 505 |
| Chain | Residue |
| A | GLY409 |
| A | ALA410 |
| A | MET411 |
| A | ASN428 |
| A | GLU429 |
| A | HIS430 |
| A | PHE431 |
| site_id | AC6 |
| Number of Residues | 29 |
| Details | binding site for residue NDP A 506 |
| Chain | Residue |
| A | LYS112 |
| A | ALA114 |
| A | THR115 |
| A | THR117 |
| A | ARG122 |
| A | ASN136 |
| A | GLU345 |
| A | HIS348 |
| A | GLY349 |
| A | THR350 |
| A | VAL351 |
| A | THR352 |
| A | ARG353 |
| A | HIS354 |
| A | ASN367 |
| A | HOH678 |
| A | HOH704 |
| A | HOH717 |
| A | HOH725 |
| A | HOH726 |
| A | HOH762 |
| A | HOH780 |
| A | HOH796 |
| A | HOH800 |
| A | HOH805 |
| A | HOH813 |
| A | HOH909 |
| A | HOH921 |
| A | HOH1008 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue NA A 507 |
| Chain | Residue |
| A | ASN136 |
| A | GLU343 |
| A | GLU345 |
| A | HOH665 |
| A | HOH719 |
| A | HOH1000 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue ACT A 508 |
| Chain | Residue |
| A | HIS453 |
| A | HIS454 |
| A | HOH608 |
| A | HOH869 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue CA A 509 |
| Chain | Residue |
| A | ASP291 |
| B | ASP314 |
| B | ASP318 |
| B | HOH705 |
| B | HOH720 |
| B | HOH782 |
| site_id | AD1 |
| Number of Residues | 8 |
| Details | binding site for residue GOL B 501 |
| Chain | Residue |
| A | PHE196 |
| A | HOH845 |
| B | VAL185 |
| B | ALA186 |
| B | ASP187 |
| B | ARG188 |
| B | HOH617 |
| B | HOH774 |
| site_id | AD2 |
| Number of Residues | 21 |
| Details | binding site for residue 69Q B 502 |
| Chain | Residue |
| A | ILE319 |
| A | LEU320 |
| B | LEU160 |
| B | TRP164 |
| B | ILE290 |
| B | VAL294 |
| B | VAL297 |
| B | LEU298 |
| B | TYR311 |
| B | ASP312 |
| B | VAL315 |
| B | GLN316 |
| B | ILE319 |
| B | LEU320 |
| B | HOH643 |
| A | ILE290 |
| A | VAL294 |
| A | TYR311 |
| A | ASP312 |
| A | VAL315 |
| A | GLN316 |
| site_id | AD3 |
| Number of Residues | 24 |
| Details | binding site for residue NDP B 503 |
| Chain | Residue |
| B | LYS112 |
| B | ALA114 |
| B | THR115 |
| B | THR117 |
| B | ARG122 |
| B | ASN136 |
| B | GLU345 |
| B | HIS348 |
| B | GLY349 |
| B | THR350 |
| B | VAL351 |
| B | THR352 |
| B | ARG353 |
| B | HIS354 |
| B | THR366 |
| B | ASN367 |
| B | ACT505 |
| B | HOH623 |
| B | HOH639 |
| B | HOH642 |
| B | HOH727 |
| B | HOH748 |
| B | HOH757 |
| B | HOH825 |
| site_id | AD4 |
| Number of Residues | 6 |
| Details | binding site for residue NA B 504 |
| Chain | Residue |
| B | ASN136 |
| B | GLU343 |
| B | GLU345 |
| B | HOH743 |
| B | HOH791 |
| B | HOH826 |
| site_id | AD5 |
| Number of Residues | 4 |
| Details | binding site for residue ACT B 505 |
| Chain | Residue |
| B | THR117 |
| B | SER134 |
| B | NDP503 |
| B | HOH602 |
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 |
