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 | 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 | 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 |