5H3E
Crystal structure of mouse isocitrate dehydrogenases 2 K256Q mutant complexed with isocitrate
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 | 0005743 | cellular_component | mitochondrial inner membrane |
| A | 0005777 | cellular_component | peroxisome |
| A | 0005829 | cellular_component | cytosol |
| 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 | 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 | 0005743 | cellular_component | mitochondrial inner membrane |
| B | 0005777 | cellular_component | peroxisome |
| B | 0005829 | cellular_component | cytosol |
| 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 | 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 | 4 |
| Details | binding site for residue MG A 501 |
| Chain | Residue |
| A | ASP314 |
| A | ASP318 |
| A | ICT502 |
| B | ASP291 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | binding site for residue ICT A 502 |
| Chain | Residue |
| A | ARG172 |
| A | TYR179 |
| A | ASP314 |
| A | MG501 |
| A | HOH644 |
| B | LYS251 |
| B | ILE254 |
| B | ASP291 |
| A | THR117 |
| A | SER134 |
| A | ASN136 |
| A | ARG140 |
| A | ARG149 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue MG B 501 |
| Chain | Residue |
| A | ASP291 |
| B | ASP314 |
| B | ASP318 |
| B | ICT502 |
| site_id | AC4 |
| Number of Residues | 13 |
| Details | binding site for residue ICT B 502 |
| Chain | Residue |
| A | LYS251 |
| A | ILE254 |
| A | ASP291 |
| B | THR117 |
| B | SER134 |
| B | ASN136 |
| B | ARG140 |
| B | ARG149 |
| B | ARG172 |
| B | TYR179 |
| B | ASP314 |
| B | ALA347 |
| B | MG501 |
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: BINDING => ECO:0000250|UniProtKB:O75874 |
| Chain | Residue | Details |
| A | ASN367 | |
| B | THR115 | |
| B | ARG122 | |
| B | LYS299 | |
| B | GLY349 | |
| B | ASN367 | |
| A | THR115 | |
| A | ARG122 | |
| A | LYS299 | |
| A | GLY349 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P33198 |
| Chain | Residue | Details |
| A | ASP291 | |
| A | ASP314 | |
| B | THR117 | |
| B | SER134 | |
| B | ARG149 | |
| B | ARG172 | |
| B | ASP291 | |
| B | ASP314 | |
| A | THR117 | |
| A | SER134 | |
| A | ARG149 | |
| A | ARG172 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | SITE: Critical for catalysis => ECO:0000250|UniProtKB:P33198 |
| Chain | Residue | Details |
| A | TYR179 | |
| A | LYS251 | |
| B | TYR179 | |
| B | LYS251 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 18 |
| Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:23576753 |
| Chain | Residue | Details |
| A | LYS199 | |
| A | LYS272 | |
| A | LYS280 | |
| A | LYS400 | |
| A | LYS442 | |
| B | LYS45 | |
| B | LYS48 | |
| B | LYS69 | |
| B | LYS155 | |
| B | LYS199 | |
| B | LYS272 | |
| B | LYS280 | |
| B | LYS400 | |
| B | LYS442 | |
| A | LYS45 | |
| A | LYS48 | |
| A | LYS69 | |
| A | LYS155 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P48735 |
| Chain | Residue | Details |
| A | LYS413 | |
| B | LYS67 | |
| B | LYS275 | |
| B | LYS413 | |
| A | LYS67 | |
| A | LYS275 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 16 |
| Details | MOD_RES: N6-succinyllysine; alternate => ECO:0007744|PubMed:23806337 |
| Chain | Residue | Details |
| A | LYS193 | |
| A | GLN256 | |
| A | LYS282 | |
| A | LYS384 | |
| B | LYS80 | |
| B | LYS106 | |
| B | LYS166 | |
| B | LYS180 | |
| B | LYS193 | |
| B | GLN256 | |
| B | LYS282 | |
| B | LYS384 | |
| A | LYS80 | |
| A | LYS106 | |
| A | LYS166 | |
| A | LYS180 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:23576753, ECO:0007744|PubMed:23806337 |
| Chain | Residue | Details |
| A | LYS263 | |
| B | LYS263 |
