2QFW
Crystal structure of Saccharomyces cerevesiae mitochondrial NADP(+)-dependent isocitrate dehydrogenase in complex 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 | 0005515 | molecular_function | protein binding |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005777 | cellular_component | peroxisome |
| A | 0005829 | cellular_component | cytosol |
| A | 0006099 | biological_process | tricarboxylic acid cycle |
| A | 0006102 | biological_process | isocitrate metabolic process |
| 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 | 0051287 | molecular_function | NAD binding |
| A | 0097054 | biological_process | L-glutamate biosynthetic process |
| 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 | 0005777 | cellular_component | peroxisome |
| B | 0005829 | cellular_component | cytosol |
| B | 0006099 | biological_process | tricarboxylic acid cycle |
| B | 0006102 | biological_process | isocitrate metabolic process |
| 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 | 0051287 | molecular_function | NAD binding |
| B | 0097054 | biological_process | L-glutamate biosynthetic process |
| 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 | 0005777 | cellular_component | peroxisome |
| C | 0005829 | cellular_component | cytosol |
| C | 0006099 | biological_process | tricarboxylic acid cycle |
| C | 0006102 | biological_process | isocitrate metabolic process |
| 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 | 0051287 | molecular_function | NAD binding |
| C | 0097054 | biological_process | L-glutamate biosynthetic process |
| 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 | 0005777 | cellular_component | peroxisome |
| D | 0005829 | cellular_component | cytosol |
| D | 0006099 | biological_process | tricarboxylic acid cycle |
| D | 0006102 | biological_process | isocitrate metabolic process |
| 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 | 0051287 | molecular_function | NAD binding |
| D | 0097054 | biological_process | L-glutamate biosynthetic process |
| E | 0000287 | molecular_function | magnesium ion binding |
| E | 0004450 | molecular_function | isocitrate dehydrogenase (NADP+) activity |
| E | 0005515 | molecular_function | protein binding |
| E | 0005739 | cellular_component | mitochondrion |
| E | 0005777 | cellular_component | peroxisome |
| E | 0005829 | cellular_component | cytosol |
| E | 0006099 | biological_process | tricarboxylic acid cycle |
| E | 0006102 | biological_process | isocitrate metabolic process |
| E | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| E | 0042645 | cellular_component | mitochondrial nucleoid |
| E | 0051287 | molecular_function | NAD binding |
| E | 0097054 | biological_process | L-glutamate biosynthetic process |
| F | 0000287 | molecular_function | magnesium ion binding |
| F | 0004450 | molecular_function | isocitrate dehydrogenase (NADP+) activity |
| F | 0005515 | molecular_function | protein binding |
| F | 0005739 | cellular_component | mitochondrion |
| F | 0005777 | cellular_component | peroxisome |
| F | 0005829 | cellular_component | cytosol |
| F | 0006099 | biological_process | tricarboxylic acid cycle |
| F | 0006102 | biological_process | isocitrate metabolic process |
| F | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| F | 0042645 | cellular_component | mitochondrial nucleoid |
| F | 0051287 | molecular_function | NAD binding |
| F | 0097054 | biological_process | L-glutamate biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE ICT A 2101 |
| Chain | Residue |
| A | THR78 |
| B | ASP254 |
| A | SER95 |
| A | ASN97 |
| A | ARG101 |
| A | ARG110 |
| A | ARG133 |
| A | TYR140 |
| A | ASP277 |
| B | LYS214 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE ICT B 2102 |
| Chain | Residue |
| A | LYS214 |
| A | ASP254 |
| B | THR78 |
| B | SER95 |
| B | ASN97 |
| B | ARG101 |
| B | ARG110 |
| B | ARG133 |
| B | TYR140 |
| B | ASP277 |
| B | HOH2305 |
| site_id | AC3 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE ICT C 2103 |
| Chain | Residue |
| C | THR78 |
| C | SER95 |
| C | ASN97 |
| C | ARG101 |
| C | ARG110 |
| C | ARG133 |
| C | TYR140 |
| C | ASP277 |
| C | HOH2131 |
| D | LYS214 |
| D | ILE217 |
| D | ASP254 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE ICT D 2104 |
| Chain | Residue |
| C | HOH2195 |
| D | SER95 |
| D | ASN97 |
| D | ARG101 |
| D | ARG110 |
| D | ARG133 |
| D | ASP277 |
| D | HOH2135 |
| D | HOH2139 |
| D | HOH2254 |
| site_id | AC5 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE ICT E 2105 |
| Chain | Residue |
| E | THR78 |
| E | SER95 |
| E | ASN97 |
| E | ARG101 |
| E | ARG110 |
| E | ARG133 |
| E | TYR140 |
| E | ASP277 |
| E | HOH2108 |
| F | LYS214 |
| F | ASP254 |
| F | HOH2141 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE ICT F 2106 |
| Chain | Residue |
| E | ILE217 |
| E | ASP254 |
| F | THR78 |
| F | SER95 |
| F | ASN97 |
| F | ARG101 |
| F | ARG110 |
| F | ARG133 |
| F | ASP277 |
| F | HOH2126 |
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 | 126 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | Site: {"description":"Critical for catalysis","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
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 | 2 |
| Details | Annotated By Reference To The Literature 1a05 |
| Chain | Residue | Details |
| D | ASP254 | |
| D | LYS214 |
| site_id | CSA11 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1a05 |
| Chain | Residue | Details |
| E | ASP254 | |
| E | LYS214 |
| site_id | CSA12 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1a05 |
| Chain | Residue | Details |
| F | ASP254 | |
| F | LYS214 |
| site_id | CSA13 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1a05 |
| Chain | Residue | Details |
| A | THR163 |
| site_id | CSA14 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1a05 |
| Chain | Residue | Details |
| B | THR163 |
| site_id | CSA15 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1a05 |
| Chain | Residue | Details |
| C | THR163 |
| site_id | CSA16 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1a05 |
| Chain | Residue | Details |
| D | THR163 |
| site_id | CSA17 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1a05 |
| Chain | Residue | Details |
| E | THR163 |
| site_id | CSA18 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1a05 |
| Chain | Residue | Details |
| F | 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 | 1 |
| Details | Annotated By Reference To The Literature 1a05 |
| Chain | Residue | Details |
| E | VAL156 |
| site_id | CSA6 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1a05 |
| Chain | Residue | Details |
| F | VAL156 |
| site_id | CSA7 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1a05 |
| Chain | Residue | Details |
| A | ASP254 | |
| A | LYS214 |
| site_id | CSA8 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1a05 |
| Chain | Residue | Details |
| B | ASP254 | |
| B | LYS214 |
| site_id | CSA9 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1a05 |
| Chain | Residue | Details |
| C | ASP254 | |
| C | LYS214 |
