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 | THR115 | |
B | ASN367 | |
A | ARG122 | |
A | LYS299 | |
A | GLY349 | |
A | ASN367 | |
B | THR115 | |
B | ARG122 | |
B | LYS299 | |
B | GLY349 |
site_id | SWS_FT_FI2 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P33198 |
Chain | Residue | Details |
A | THR117 | |
B | ARG172 | |
B | ASP291 | |
B | ASP314 | |
A | SER134 | |
A | ARG149 | |
A | ARG172 | |
A | ASP291 | |
A | ASP314 | |
B | THR117 | |
B | SER134 | |
B | ARG149 |
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 | LYS45 | |
B | LYS45 | |
B | LYS48 | |
B | LYS69 | |
B | LYS155 | |
B | LYS199 | |
B | LYS272 | |
B | LYS280 | |
B | LYS400 | |
B | LYS442 | |
A | LYS48 | |
A | LYS69 | |
A | LYS155 | |
A | LYS199 | |
A | LYS272 | |
A | LYS280 | |
A | LYS400 | |
A | LYS442 |
site_id | SWS_FT_FI5 |
Number of Residues | 6 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P48735 |
Chain | Residue | Details |
A | LYS67 | |
A | LYS275 | |
A | LYS413 | |
B | LYS67 | |
B | LYS275 | |
B | LYS413 |
site_id | SWS_FT_FI6 |
Number of Residues | 16 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0007744|PubMed:23806337 |
Chain | Residue | Details |
A | LYS80 | |
B | LYS106 | |
B | LYS166 | |
B | LYS180 | |
B | LYS193 | |
B | GLN256 | |
B | LYS282 | |
B | LYS384 | |
A | LYS106 | |
A | LYS166 | |
A | LYS180 | |
A | LYS193 | |
A | GLN256 | |
A | LYS282 | |
A | LYS384 | |
B | LYS80 |
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 |