6AJ8
Crystal structure of Trypanosoma brucei glycosomal isocitrate dehydrogenase in complex with NADP+, alpha-ketoglutarate and ca2+
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 | 0005737 | cellular_component | cytoplasm |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0006099 | biological_process | tricarboxylic acid cycle |
| A | 0006102 | biological_process | isocitrate metabolic process |
| A | 0006739 | biological_process | NADP+ metabolic process |
| 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 | 0020015 | cellular_component | glycosome |
| 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 | 0005737 | cellular_component | cytoplasm |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0006099 | biological_process | tricarboxylic acid cycle |
| B | 0006102 | biological_process | isocitrate metabolic process |
| B | 0006739 | biological_process | NADP+ metabolic process |
| 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 | 0020015 | cellular_component | glycosome |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 20 |
| Details | binding site for residue NAP A 501 |
| Chain | Residue |
| A | LYS72 |
| A | THR310 |
| A | VAL311 |
| A | THR312 |
| A | ARG313 |
| A | HIS314 |
| A | THR326 |
| A | ASN327 |
| A | HOH604 |
| A | HOH615 |
| A | HOH654 |
| A | THR75 |
| A | HOH664 |
| A | ILE76 |
| A | THR77 |
| A | ARG82 |
| A | ASN96 |
| A | GLU305 |
| A | HIS308 |
| A | GLY309 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue CA A 502 |
| Chain | Residue |
| A | ASP274 |
| A | ASP278 |
| B | ASP251 |
| B | HOH679 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue CA A 503 |
| Chain | Residue |
| A | ASP251 |
| B | ASP274 |
| B | ASP278 |
| B | HOH685 |
| site_id | AC4 |
| Number of Residues | 16 |
| Details | binding site for residue NAP B 501 |
| Chain | Residue |
| B | LYS72 |
| B | THR75 |
| B | ILE76 |
| B | THR77 |
| B | ARG82 |
| B | ASN96 |
| B | GLU305 |
| B | HIS308 |
| B | GLY309 |
| B | THR310 |
| B | VAL311 |
| B | THR312 |
| B | HIS314 |
| B | THR326 |
| B | ASN327 |
| B | HOH668 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue AKG B 502 |
| Chain | Residue |
| B | SER94 |
| B | ASN96 |
| B | ARG100 |
| B | ARG132 |
| B | HOH633 |
| B | HOH661 |
Functional Information from PROSITE/UniProt
| site_id | PS00470 |
| Number of Residues | 20 |
| Details | IDH_IMDH Isocitrate and isopropylmalate dehydrogenases signature. NYDGDVqSDslAqgf.GSLGM |
| Chain | Residue | Details |
| A | ASN270-MET289 |
