6AJA
Crystal structure of Trypanosoma brucei glycosomal isocitrate dehydrogenase in complex with NADPH, 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 |
C | 0000166 | molecular_function | nucleotide binding |
C | 0000287 | molecular_function | magnesium ion binding |
C | 0004450 | molecular_function | isocitrate dehydrogenase (NADP+) activity |
C | 0005739 | cellular_component | mitochondrion |
C | 0006099 | biological_process | tricarboxylic acid cycle |
C | 0006102 | biological_process | isocitrate metabolic process |
C | 0006739 | biological_process | NADP metabolic process |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
C | 0020015 | cellular_component | glycosome |
C | 0046872 | molecular_function | metal ion binding |
C | 0051287 | molecular_function | NAD binding |
D | 0000166 | molecular_function | nucleotide binding |
D | 0000287 | molecular_function | magnesium ion binding |
D | 0004450 | molecular_function | isocitrate dehydrogenase (NADP+) activity |
D | 0005739 | cellular_component | mitochondrion |
D | 0006099 | biological_process | tricarboxylic acid cycle |
D | 0006102 | biological_process | isocitrate metabolic process |
D | 0006739 | biological_process | NADP metabolic process |
D | 0016491 | molecular_function | oxidoreductase activity |
D | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
D | 0020015 | cellular_component | glycosome |
D | 0046872 | molecular_function | metal ion binding |
D | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 15 |
Details | binding site for residue NAP A 501 |
Chain | Residue |
A | LYS72 |
A | VAL311 |
A | THR312 |
A | ARG313 |
A | HIS314 |
A | ASN327 |
A | HOH620 |
A | THR75 |
A | ILE76 |
A | THR77 |
A | ARG82 |
A | ASN96 |
A | HIS308 |
A | GLY309 |
A | THR310 |
site_id | AC2 |
Number of Residues | 3 |
Details | binding site for residue CA A 502 |
Chain | Residue |
A | ASP274 |
A | ASP278 |
B | ASP251 |
site_id | AC3 |
Number of Residues | 1 |
Details | binding site for residue GOL A 503 |
Chain | Residue |
A | ASP360 |
site_id | AC4 |
Number of Residues | 1 |
Details | binding site for residue GOL A 504 |
Chain | Residue |
A | PRO118 |
site_id | AC5 |
Number of Residues | 3 |
Details | binding site for residue CA A 505 |
Chain | Residue |
A | ASP251 |
B | ASP274 |
B | ASP278 |
site_id | AC6 |
Number of Residues | 13 |
Details | binding site for residue NAP B 501 |
Chain | Residue |
B | THR75 |
B | ILE76 |
B | THR77 |
B | ASN96 |
B | GLU305 |
B | HIS308 |
B | GLY309 |
B | THR310 |
B | VAL311 |
B | THR312 |
B | ARG313 |
B | HIS314 |
B | ASN327 |
site_id | AC7 |
Number of Residues | 19 |
Details | binding site for residue NAP C 501 |
Chain | Residue |
C | LYS72 |
C | ALA74 |
C | THR75 |
C | ILE76 |
C | THR77 |
C | ARG82 |
C | ASN96 |
C | GLY288 |
C | GLU305 |
C | HIS308 |
C | GLY309 |
C | THR310 |
C | VAL311 |
C | THR312 |
C | ARG313 |
C | HIS314 |
C | THR326 |
C | ASN327 |
C | HOH607 |
site_id | AC8 |
Number of Residues | 2 |
Details | binding site for residue CA C 502 |
Chain | Residue |
C | ASP274 |
C | ASP278 |
site_id | AC9 |
Number of Residues | 7 |
Details | binding site for residue GOL C 503 |
Chain | Residue |
C | GLN138 |
C | ASP219 |
C | LYS269 |
C | TYR271 |
C | ASP272 |
D | GLN138 |
D | TYR271 |
site_id | AD1 |
Number of Residues | 2 |
Details | binding site for residue GOL C 504 |
Chain | Residue |
C | LYS27 |
C | TYR41 |
site_id | AD2 |
Number of Residues | 21 |
Details | binding site for residue NAP D 501 |
Chain | Residue |
C | LEU249 |
C | ASP252 |
C | ARG259 |
D | LYS72 |
D | ALA74 |
D | THR75 |
D | THR77 |
D | ARG82 |
D | ASN96 |
D | LEU287 |
D | GLU305 |
D | HIS308 |
D | GLY309 |
D | THR310 |
D | VAL311 |
D | THR312 |
D | ARG313 |
D | HIS314 |
D | THR326 |
D | ASN327 |
D | AKG503 |
site_id | AD3 |
Number of Residues | 4 |
Details | binding site for residue CA D 502 |
Chain | Residue |
D | ARG109 |
D | ASP274 |
D | ASP278 |
D | AKG503 |
site_id | AD4 |
Number of Residues | 12 |
Details | binding site for residue AKG D 503 |
Chain | Residue |
D | ASP274 |
D | ALA307 |
D | NAP501 |
D | CA502 |
C | LYS211 |
C | ILE214 |
D | THR77 |
D | SER94 |
D | ASN96 |
D | ARG100 |
D | ARG109 |
D | ARG132 |
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 |