Functional Information from GO Data
| Chain | GOid | namespace | contents | 
| A | 0000166 | molecular_function | nucleotide binding | 
| A | 0000287 | molecular_function | magnesium ion binding | 
| A | 0004450 | molecular_function | isocitrate dehydrogenase (NADP+) activity | 
| A | 0006097 | biological_process | glyoxylate cycle | 
| A | 0006099 | biological_process | tricarboxylic acid cycle | 
| 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 | 
| B | 0000166 | molecular_function | nucleotide binding | 
| B | 0000287 | molecular_function | magnesium ion binding | 
| B | 0004450 | molecular_function | isocitrate dehydrogenase (NADP+) activity | 
| B | 0006097 | biological_process | glyoxylate cycle | 
| B | 0006099 | biological_process | tricarboxylic acid cycle | 
| 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 | 
Functional Information from PDB Data
| site_id | AC1 | 
| Number of Residues | 5 | 
| Details | BINDING SITE FOR RESIDUE CA A 1005 | 
| Chain | Residue | 
| A | ASP287 | 
| B | ASP311 | 
| B | ICT1004 | 
| B | HOH1005 | 
| B | HOH1006 | 
| site_id | AC2 | 
| Number of Residues | 7 | 
| Details | BINDING SITE FOR RESIDUE CA A 1006 | 
| Chain | Residue | 
| A | HOH1136 | 
| A | HOH1137 | 
| B | ASP287 | 
| A | ASP311 | 
| A | ASP315 | 
| A | ICT1002 | 
| A | HOH1135 | 
| site_id | AC3 | 
| Number of Residues | 18 | 
| Details | BINDING SITE FOR RESIDUE NAP A 1001 | 
| Chain | Residue | 
| A | LYS107 | 
| A | PRO109 | 
| A | LEU110 | 
| A | THR112 | 
| A | ASN122 | 
| A | GLY325 | 
| A | GLU340 | 
| A | PRO341 | 
| A | VAL342 | 
| A | HIS343 | 
| A | GLY344 | 
| A | THR345 | 
| A | ALA346 | 
| A | TYR349 | 
| A | ILE355 | 
| A | ASN356 | 
| A | ASP397 | 
| A | ARG400 | 
| site_id | AC4 | 
| Number of Residues | 9 | 
| Details | BINDING SITE FOR RESIDUE ICT A 1002 | 
| Chain | Residue | 
| A | ARG136 | 
| A | ARG159 | 
| A | TYR166 | 
| A | ASP311 | 
| A | CA1006 | 
| A | HOH1136 | 
| B | LYS233 | 
| B | ASN235 | 
| B | ASP287 | 
| site_id | AC5 | 
| Number of Residues | 28 | 
| Details | BINDING SITE FOR RESIDUE NAP B 1003 | 
| Chain | Residue | 
| A | ASN235 | 
| A | ILE285 | 
| A | ASN288 | 
| A | GLN291 | 
| A | GLN292 | 
| A | ARG296 | 
| B | PRO109 | 
| B | LEU110 | 
| B | THR112 | 
| B | ASN122 | 
| B | ARG126 | 
| B | ILE324 | 
| B | GLY325 | 
| B | GLU340 | 
| B | VAL342 | 
| B | HIS343 | 
| B | GLY344 | 
| B | THR345 | 
| B | ALA346 | 
| B | LYS348 | 
| B | TYR349 | 
| B | ILE355 | 
| B | ASN356 | 
| B | ASP397 | 
| B | ICT1004 | 
| B | HOH1008 | 
| B | HOH1009 | 
| B | HOH1010 | 
| site_id | AC6 | 
| Number of Residues | 14 | 
| Details | BINDING SITE FOR RESIDUE ICT B 1004 | 
| Chain | Residue | 
| A | LYS233 | 
| A | ASP287 | 
| A | CA1005 | 
| B | THR112 | 
| B | SER120 | 
| B | ASN122 | 
| B | ARG126 | 
| B | ARG136 | 
| B | ARG159 | 
| B | TYR166 | 
| B | ASP311 | 
| B | NAP1003 | 
| B | HOH1005 | 
| B | HOH1007 | 
Functional Information from PROSITE/UniProt
| site_id | PS00470 | 
| Number of Residues | 20 | 
| Details | IDH_IMDH Isocitrate and isopropylmalate dehydrogenases signature. NLNGDYiSDaaSalv.GGIGM | 
| Chain | Residue | Details | 
| A | ASN307-MET326 |  | 
Catalytic Information from CSA
| site_id | CSA1 | 
| Number of Residues | 3 | 
| Details | Annotated By Reference To The Literature 1a05 | 
| Chain | Residue | Details | 
| A | ASP287 |  | 
| A | LYS233 |  | 
| B | TYR166 |  | 
| site_id | CSA2 | 
| Number of Residues | 3 | 
| Details | Annotated By Reference To The Literature 1a05 | 
| Chain | Residue | Details | 
| A | TYR166 |  | 
| B | ASP287 |  | 
| B | LYS233 |  |