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 | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0006097 | biological_process | glyoxylate cycle |
A | 0006099 | biological_process | tricarboxylic acid cycle |
A | 0006979 | biological_process | response to oxidative stress |
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 | 0022900 | biological_process | electron transport chain |
A | 0046872 | molecular_function | metal ion binding |
A | 0051287 | molecular_function | NAD binding |
A | 0097216 | molecular_function | guanosine tetraphosphate binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE A2P A 501 |
Chain | Residue |
A | ARG292 |
A | TYR391 |
A | ASP392 |
A | HOH2358 |
A | HOH2366 |
A | HOH2424 |
A | HOH2425 |
A | HOH2426 |
A | HIS339 |
A | GLY340 |
A | THR341 |
A | ALA342 |
A | LYS344 |
A | TYR345 |
A | VAL351 |
A | ASN352 |
site_id | AC2 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE AKG A 502 |
Chain | Residue |
A | SER113 |
A | ASN115 |
A | ARG119 |
A | ARG129 |
A | ARG153 |
A | TYR160 |
A | LYS230 |
A | ASN232 |
A | ILE233 |
A | ASP307 |
A | CA503 |
A | HOH2168 |
A | HOH2287 |
A | HOH2428 |
site_id | AC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE CA A 503 |
Chain | Residue |
A | ASP283 |
A | ASP307 |
A | ASP311 |
A | AKG502 |
A | HOH2169 |
A | HOH2350 |
A | HOH2429 |
site_id | AC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 A 504 |
Chain | Residue |
A | VAL107 |
A | GLY108 |
A | GLY109 |
A | GLY110 |
A | LYS235 |
A | HOH2138 |
A | HOH2143 |
Functional Information from PROSITE/UniProt
site_id | PS00470 |
Number of Residues | 20 |
Details | IDH_IMDH Isocitrate and isopropylmalate dehydrogenases signature. NLNGDYiSDalAaqv.GGIGI |
Chain | Residue | Details |
A | ASN303-ILE322 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"10623532","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1CW1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1CW4","evidenceCode":"ECO:0007744"}]} |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 4 |
Details | M-CSA 7 |
Chain | Residue | Details |
A | TYR160 | electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor, proton relay |
A | LYS230 | electrostatic stabiliser, proton acceptor, proton donor, proton relay |
A | ASP283 | electrostatic stabiliser, proton acceptor, proton donor |
A | ASP307 | metal ligand |