5I95
Crystal Structure of Human Mitochondrial Isocitrate Dehydrogenase R140Q Mutant Homodimer bound to NADPH and alpha-Ketoglutaric acid
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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 34 |
| Details | binding site for residue NDP A 501 |
| Chain | Residue |
| A | LYS112 |
| A | GLN296 |
| A | LYS299 |
| A | HIS348 |
| A | GLY349 |
| A | THR350 |
| A | VAL351 |
| A | THR352 |
| A | ARG353 |
| A | HIS354 |
| A | ASN367 |
| A | ALA114 |
| A | AKG508 |
| A | HOH665 |
| A | HOH683 |
| A | HOH711 |
| A | HOH724 |
| A | HOH733 |
| A | HOH746 |
| A | HOH761 |
| A | HOH776 |
| A | HOH780 |
| A | THR115 |
| A | HOH785 |
| A | HOH786 |
| A | HOH811 |
| A | HOH880 |
| A | HOH948 |
| A | ILE116 |
| A | THR117 |
| A | ARG122 |
| A | ASN136 |
| A | LEU289 |
| A | ASP292 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue CA A 502 |
| Chain | Residue |
| A | ARG149 |
| A | ASP291 |
| A | ASP314 |
| A | ASP318 |
| A | AKG508 |
| A | HOH619 |
| A | HOH658 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | binding site for residue GOL A 503 |
| Chain | Residue |
| A | PHE184 |
| A | VAL185 |
| A | ALA186 |
| A | ASP187 |
| A | ARG188 |
| A | PHE196 |
| A | HOH640 |
| A | HOH668 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 504 |
| Chain | Residue |
| A | PHE148 |
| A | GLU150 |
| A | TYR238 |
| A | ARG377 |
| A | HOH629 |
| A | HOH791 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue GOL A 505 |
| Chain | Residue |
| A | LYS280 |
| A | LYS282 |
| A | GOL506 |
| A | HOH769 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 506 |
| Chain | Residue |
| A | MET397 |
| A | GLU404 |
| A | ARG451 |
| A | GOL505 |
| A | HOH617 |
| A | HOH920 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | binding site for residue ACT A 507 |
| Chain | Residue |
| A | LYS413 |
| A | PHE431 |
| site_id | AC8 |
| Number of Residues | 16 |
| Details | binding site for residue AKG A 508 |
| Chain | Residue |
| A | THR117 |
| A | SER134 |
| A | ASN136 |
| A | ARG149 |
| A | ARG172 |
| A | LYS251 |
| A | ILE254 |
| A | ASP291 |
| A | ASP314 |
| A | ALA347 |
| A | NDP501 |
| A | CA502 |
| A | HOH632 |
| A | HOH658 |
| A | HOH733 |
| A | HOH822 |
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 | 10 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"O75874","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 11 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P33198","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| 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 | 6 |
| 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 | 6 |
| 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 | 8 |
| 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 | 1 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"22416140","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
