2QFV
Crystal structure of Saccharomyces cerevesiae mitochondrial NADP(+)-dependent isocitrate dehydrogenase in complex with NADP(+)
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 | 0005515 | molecular_function | protein binding |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0006097 | biological_process | glyoxylate cycle |
| A | 0006099 | biological_process | tricarboxylic acid cycle |
| A | 0006102 | biological_process | isocitrate metabolic process |
| A | 0006537 | biological_process | glutamate biosynthetic process |
| A | 0006739 | biological_process | NADP metabolic 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 | 0042645 | cellular_component | mitochondrial nucleoid |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051287 | molecular_function | NAD binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0004450 | molecular_function | isocitrate dehydrogenase (NADP+) activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0006097 | biological_process | glyoxylate cycle |
| B | 0006099 | biological_process | tricarboxylic acid cycle |
| B | 0006102 | biological_process | isocitrate metabolic process |
| B | 0006537 | biological_process | glutamate biosynthetic process |
| B | 0006739 | biological_process | NADP metabolic 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 | 0042645 | cellular_component | mitochondrial nucleoid |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051287 | molecular_function | NAD binding |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0004450 | molecular_function | isocitrate dehydrogenase (NADP+) activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0005739 | cellular_component | mitochondrion |
| C | 0006097 | biological_process | glyoxylate cycle |
| C | 0006099 | biological_process | tricarboxylic acid cycle |
| C | 0006102 | biological_process | isocitrate metabolic process |
| C | 0006537 | biological_process | glutamate biosynthetic process |
| C | 0006739 | biological_process | NADP metabolic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| C | 0042645 | cellular_component | mitochondrial nucleoid |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0051287 | molecular_function | NAD binding |
| D | 0000287 | molecular_function | magnesium ion binding |
| D | 0004450 | molecular_function | isocitrate dehydrogenase (NADP+) activity |
| D | 0005515 | molecular_function | protein binding |
| D | 0005739 | cellular_component | mitochondrion |
| D | 0006097 | biological_process | glyoxylate cycle |
| D | 0006099 | biological_process | tricarboxylic acid cycle |
| D | 0006102 | biological_process | isocitrate metabolic process |
| D | 0006537 | biological_process | glutamate biosynthetic process |
| D | 0006739 | biological_process | NADP metabolic process |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| D | 0042645 | cellular_component | mitochondrial nucleoid |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE NAP A 1001 |
| Chain | Residue |
| A | LYS73 |
| A | GLY312 |
| A | THR313 |
| A | THR315 |
| A | ARG316 |
| A | HIS317 |
| A | ASN330 |
| A | HOH1007 |
| A | HOH1061 |
| A | HOH1075 |
| A | HOH1145 |
| A | ALA75 |
| A | HOH1204 |
| D | GLN59 |
| A | THR76 |
| A | ILE77 |
| A | THR78 |
| A | ARG83 |
| A | ASN97 |
| A | GLU308 |
| A | HIS311 |
| site_id | AC2 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE NAP B 1002 |
| Chain | Residue |
| B | LYS73 |
| B | ALA75 |
| B | THR76 |
| B | ILE77 |
| B | THR78 |
| B | ASN97 |
| B | GLU308 |
| B | HIS311 |
| B | GLY312 |
| B | THR313 |
| B | ARG316 |
| B | HIS317 |
| B | ASN330 |
| B | HOH1014 |
| B | HOH1067 |
| B | HOH1181 |
| site_id | AC3 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE NAP C 1003 |
| Chain | Residue |
| C | LYS73 |
| C | ALA75 |
| C | THR76 |
| C | ILE77 |
| C | THR78 |
| C | ARG83 |
| C | ASN97 |
| C | GLU308 |
| C | HIS311 |
| C | GLY312 |
| C | THR313 |
| C | THR315 |
| C | ARG316 |
| C | HIS317 |
| C | THR329 |
| C | ASN330 |
| C | HOH1033 |
| C | HOH1053 |
| C | HOH1154 |
| C | HOH1208 |
| site_id | AC4 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE NAP D 1004 |
| Chain | Residue |
| A | GLN59 |
| D | LYS73 |
| D | ALA75 |
| D | THR76 |
| D | ILE77 |
| D | THR78 |
| D | ARG83 |
| D | ASN97 |
| D | GLU308 |
| D | HIS311 |
| D | GLY312 |
| D | THR313 |
| D | THR315 |
| D | ARG316 |
| D | HIS317 |
| D | THR329 |
| D | ASN330 |
| D | HOH1029 |
| D | HOH1030 |
| D | HOH1080 |
| D | HOH1161 |
Functional Information from PROSITE/UniProt
| site_id | PS00470 |
| Number of Residues | 20 |
| Details | IDH_IMDH Isocitrate and isopropylmalate dehydrogenases signature. NYDGDVqSDivAqgf.GSLGL |
| Chain | Residue | Details |
| A | ASN273-LEU292 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 44 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | THR76 | |
| A | GLY312 | |
| A | ASN330 | |
| B | THR76 | |
| B | THR78 | |
| B | ARG83 | |
| B | SER95 | |
| B | ARG110 | |
| B | ARG133 | |
| B | ASP254 | |
| B | LYS262 | |
| A | THR78 | |
| B | ASP277 | |
| B | GLY312 | |
| B | ASN330 | |
| C | THR76 | |
| C | THR78 | |
| C | ARG83 | |
| C | SER95 | |
| C | ARG110 | |
| C | ARG133 | |
| C | ASP254 | |
| A | ARG83 | |
| C | LYS262 | |
| C | ASP277 | |
| C | GLY312 | |
| C | ASN330 | |
| D | THR76 | |
| D | THR78 | |
| D | ARG83 | |
| D | SER95 | |
| D | ARG110 | |
| D | ARG133 | |
| A | SER95 | |
| D | ASP254 | |
| D | LYS262 | |
| D | ASP277 | |
| D | GLY312 | |
| D | ASN330 | |
| A | ARG110 | |
| A | ARG133 | |
| A | ASP254 | |
| A | LYS262 | |
| A | ASP277 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | SITE: Critical for catalysis => ECO:0000250 |
| Chain | Residue | Details |
| A | TYR140 | |
| A | LYS214 | |
| B | TYR140 | |
| B | LYS214 | |
| C | TYR140 | |
| C | LYS214 | |
| D | TYR140 | |
| D | LYS214 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1a05 |
| Chain | Residue | Details |
| A | VAL156 |
| site_id | CSA10 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1a05 |
| Chain | Residue | Details |
| B | THR163 |
| site_id | CSA11 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1a05 |
| Chain | Residue | Details |
| C | THR163 |
| site_id | CSA12 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1a05 |
| Chain | Residue | Details |
| D | THR163 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1a05 |
| Chain | Residue | Details |
| B | VAL156 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1a05 |
| Chain | Residue | Details |
| C | VAL156 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1a05 |
| Chain | Residue | Details |
| D | VAL156 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1a05 |
| Chain | Residue | Details |
| A | ASP254 | |
| A | LYS214 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1a05 |
| Chain | Residue | Details |
| B | ASP254 | |
| B | LYS214 |
| site_id | CSA7 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1a05 |
| Chain | Residue | Details |
| C | ASP254 | |
| C | LYS214 |
| site_id | CSA8 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1a05 |
| Chain | Residue | Details |
| D | ASP254 | |
| D | LYS214 |
| site_id | CSA9 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1a05 |
| Chain | Residue | Details |
| A | THR163 |
