4JA8
Complex of Mitochondrial Isocitrate Dehydrogenase R140Q Mutant with AGI-6780 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 | 26 |
| Details | BINDING SITE FOR RESIDUE NDP A 501 |
| Chain | Residue |
| A | LYS112 |
| A | GLY349 |
| A | THR350 |
| A | VAL351 |
| A | THR352 |
| A | ARG353 |
| A | HIS354 |
| A | ASN367 |
| A | GOL505 |
| A | HOH608 |
| A | HOH642 |
| A | ALA114 |
| A | HOH659 |
| A | HOH668 |
| A | HOH686 |
| A | HOH692 |
| A | HOH784 |
| A | HOH874 |
| A | HOH980 |
| A | THR115 |
| A | ILE116 |
| A | THR117 |
| A | ARG122 |
| A | ASN136 |
| A | GLU345 |
| A | HIS348 |
| site_id | AC2 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE 1K9 A 502 |
| Chain | Residue |
| A | TRP164 |
| A | VAL294 |
| A | VAL297 |
| A | LEU298 |
| A | TRP306 |
| A | TYR311 |
| A | ASP312 |
| A | VAL315 |
| A | GLN316 |
| A | ILE319 |
| A | LEU320 |
| B | TRP164 |
| B | VAL294 |
| B | VAL297 |
| B | LEU298 |
| B | TRP306 |
| B | TYR311 |
| B | ASP312 |
| B | VAL315 |
| B | GLN316 |
| B | ILE319 |
| B | LEU320 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 503 |
| Chain | Residue |
| A | ASP314 |
| A | ASP318 |
| A | HOH871 |
| B | ASP291 |
| B | HOH601 |
| B | HOH602 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 504 |
| Chain | Residue |
| A | ASP271 |
| A | LYS272 |
| A | HIS273 |
| A | TYR274 |
| A | LYS275 |
| A | THR276 |
| A | HOH799 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 505 |
| Chain | Residue |
| A | THR117 |
| A | SER134 |
| A | ASN136 |
| A | NDP501 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 506 |
| Chain | Residue |
| A | VAL185 |
| A | ALA186 |
| A | ASP187 |
| A | ARG188 |
| A | HOH954 |
| B | PHE196 |
| B | LYS205 |
| B | HOH735 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 507 |
| Chain | Residue |
| A | LYS280 |
| A | LYS282 |
| A | GLU404 |
| A | ASN444 |
| A | HOH660 |
| A | HOH739 |
| A | HOH830 |
| A | HOH1019 |
| site_id | AC8 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE NDP B 501 |
| Chain | Residue |
| B | HOH704 |
| B | HOH765 |
| B | HOH781 |
| B | HOH800 |
| B | HOH839 |
| B | HOH864 |
| B | LYS112 |
| B | ALA114 |
| B | THR115 |
| B | THR117 |
| B | ARG122 |
| B | ASN136 |
| B | LEU327 |
| B | GLU345 |
| B | HIS348 |
| B | GLY349 |
| B | THR350 |
| B | VAL351 |
| B | THR352 |
| B | ARG353 |
| B | HIS354 |
| B | ASN367 |
| B | HOH673 |
| B | HOH685 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA B 502 |
| Chain | Residue |
| A | ASP291 |
| A | HOH601 |
| B | ASP314 |
| B | ASP318 |
| B | HOH603 |
| B | HOH819 |
| B | HOH847 |
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 | 12 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P54071 |
| Chain | Residue | Details |
| A | LYS45 | |
| B | LYS199 | |
| B | LYS280 | |
| B | LYS400 | |
| A | LYS48 | |
| A | LYS69 | |
| A | LYS199 | |
| A | LYS280 | |
| A | LYS400 | |
| B | LYS45 | |
| B | LYS48 | |
| B | LYS69 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 12 |
| Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
| Chain | Residue | Details |
| A | LYS67 | |
| B | LYS272 | |
| B | LYS275 | |
| B | LYS442 | |
| A | LYS155 | |
| A | LYS263 | |
| A | LYS272 | |
| A | LYS275 | |
| A | LYS442 | |
| B | LYS67 | |
| B | LYS155 | |
| B | LYS263 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 16 |
| Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P54071 |
| Chain | Residue | Details |
| A | LYS80 | |
| B | LYS106 | |
| B | LYS166 | |
| B | LYS180 | |
| B | LYS193 | |
| B | LYS256 | |
| B | LYS282 | |
| B | LYS384 | |
| A | LYS106 | |
| A | LYS166 | |
| A | LYS180 | |
| A | LYS193 | |
| A | LYS256 | |
| A | LYS282 | |
| A | LYS384 | |
| B | LYS80 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:22416140 |
| Chain | Residue | Details |
| A | LYS413 | |
| B | LYS413 |
