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 | 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 | 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 | 43 |
| Details | binding site for residue EE1 A 501 |
| Chain | Residue |
| A | ILE43 |
| A | ARG135 |
| A | ARG159 |
| A | TYR166 |
| A | ASP313 |
| A | ILE326 |
| A | GLU342 |
| A | THR344 |
| A | HIS345 |
| A | GLY346 |
| A | THR347 |
| A | LYS106 |
| A | ALA348 |
| A | LYS350 |
| A | TYR351 |
| A | VAL357 |
| A | ASN358 |
| A | TYR397 |
| A | ASP398 |
| A | HOH602 |
| A | HOH618 |
| A | HOH627 |
| A | PRO108 |
| A | HOH671 |
| A | HOH672 |
| A | HOH702 |
| A | HOH760 |
| A | HOH775 |
| A | HOH877 |
| A | HOH894 |
| A | HOH931 |
| B | LYS236 |
| B | ASN238 |
| A | LEU109 |
| B | ILE287 |
| B | ASP289 |
| B | GLN294 |
| B | ARG298 |
| A | THR110 |
| A | THR111 |
| A | SER119 |
| A | ASN121 |
| A | ARG125 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue GLY A 502 |
| Chain | Residue |
| A | VAL21 |
| A | ASP336 |
| A | GLN337 |
| A | MET338 |
| A | HOH611 |
| A | HOH796 |
| A | HOH905 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue GLY A 503 |
| Chain | Residue |
| A | GLU387 |
| A | HOH625 |
| A | HOH662 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue GLY A 504 |
| Chain | Residue |
| A | ALA22 |
| A | SER26 |
| A | LEU27 |
| A | HIS28 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue CL A 505 |
| Chain | Residue |
| A | LYS79 |
| A | LYS79 |
| A | LYS82 |
| A | LYS82 |
| site_id | AC6 |
| Number of Residues | 42 |
| Details | binding site for residue EE1 B 500 |
| Chain | Residue |
| B | HOH757 |
| B | HOH805 |
| B | HOH824 |
| B | HOH835 |
| A | LYS236 |
| A | ASN238 |
| A | ILE287 |
| A | ASP289 |
| A | GLN294 |
| A | ARG298 |
| B | ILE43 |
| B | PRO108 |
| B | LEU109 |
| B | THR110 |
| B | THR111 |
| B | SER119 |
| B | ASN121 |
| B | ARG125 |
| B | ARG135 |
| B | ARG159 |
| B | TYR166 |
| B | ASP313 |
| B | ILE326 |
| B | GLY327 |
| B | GLU342 |
| B | THR344 |
| B | HIS345 |
| B | GLY346 |
| B | THR347 |
| B | ALA348 |
| B | LYS350 |
| B | TYR351 |
| B | VAL357 |
| B | ASN358 |
| B | TYR397 |
| B | ASP398 |
| B | HOH601 |
| B | HOH620 |
| B | HOH627 |
| B | HOH660 |
| B | HOH661 |
| B | HOH668 |
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 | ASN309-ILE328 | |
