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 | 2 |
| Details | BINDING SITE FOR RESIDUE ZN A1413 |
| Chain | Residue |
| A | ASP26 |
| A | HOH2066 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE ZN A1414 |
| Chain | Residue |
| A | HIS388 |
| A | GLY393 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A1415 |
| Chain | Residue |
| A | ASP301 |
| A | ASP305 |
| A | CL1418 |
| B | ASP277 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE ZN A1416 |
| Chain | Residue |
| A | LYS200 |
| A | GLU196 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL A1418 |
| Chain | Residue |
| A | ZN1415 |
| B | ASP277 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ZN B1413 |
| Chain | Residue |
| B | ARG399 |
| B | GLU400 |
| B | HOH2028 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B1414 |
| Chain | Residue |
| A | ASP277 |
| B | ASP301 |
| B | ASP305 |
| B | CL1418 |
| site_id | AC8 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE ZN B1415 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE ZN B1416 |
| Chain | Residue |
| B | GLU196 |
| B | LYS200 |
| site_id | BC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ZN B1417 |
| Chain | Residue |
| B | HIS139 |
| B | GLU141 |
| B | LYS142 |
| site_id | BC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL B1418 |
| Chain | Residue |
| A | ASP277 |
| B | ZN1414 |
| B | HOH2023 |
Functional Information from PROSITE/UniProt
| site_id | PS00470 |
| Number of Residues | 20 |
| Details | IDH_IMDH Isocitrate and isopropylmalate dehydrogenases signature. NLNGDYlSDaaAali.GGLGI |
| Chain | Residue | Details |
| A | ASN297-ILE316 | |
Functional Information from SwissProt/UniProt
| Chain | Residue | Details |
| A | THR100 | |
| A | TYR385 | |
| A | ARG389 | |
| B | THR100 | |
| B | SER109 | |
| B | ASN111 | |
| B | ARG115 | |
| B | ARG125 | |
| B | ARG149 | |
| B | ASP301 | |
| B | HIS333 | |
| A | SER109 | |
| B | ASN346 | |
| B | TYR385 | |
| B | ARG389 | |
| A | ASN111 | |
| A | ARG115 | |
| A | ARG125 | |
| A | ARG149 | |
| A | ASP301 | |
| A | HIS333 | |
| A | ASN346 | |
| Chain | Residue | Details |
| A | TYR156 | |
| A | LYS223 | |
| B | TYR156 | |
| B | LYS223 | |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1a05 |
| Chain | Residue | Details |
| A | LYS223 | |
| A | ASP277 | |
| B | TYR156 | |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1a05 |
| Chain | Residue | Details |
| A | TYR156 | |
| B | ASP277 | |
| B | LYS223 | |
