6LKY
Crystal structure of isocitrate dehydrogenase from Methylococcus capsulatus
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0000287 | molecular_function | magnesium ion binding |
A | 0004449 | molecular_function | isocitrate dehydrogenase (NAD+) activity |
A | 0006099 | biological_process | tricarboxylic acid cycle |
A | 0006102 | biological_process | isocitrate metabolic process |
A | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
A | 0051287 | molecular_function | NAD binding |
B | 0000166 | molecular_function | nucleotide binding |
B | 0000287 | molecular_function | magnesium ion binding |
B | 0004449 | molecular_function | isocitrate dehydrogenase (NAD+) activity |
B | 0006099 | biological_process | tricarboxylic acid cycle |
B | 0006102 | biological_process | isocitrate metabolic process |
B | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
B | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 28 |
Details | binding site for residue NAD A 501 |
Chain | Residue |
A | LYS66 |
A | VAL262 |
A | HIS263 |
A | GLY264 |
A | SER265 |
A | ALA266 |
A | ASP268 |
A | ILE269 |
A | ASN276 |
A | ACE502 |
A | CIT503 |
A | PRO68 |
A | HOH620 |
A | HOH626 |
A | HOH682 |
A | HOH684 |
A | HOH710 |
B | ASN176 |
B | ILE205 |
B | ALA208 |
B | HOH532 |
A | LEU69 |
A | THR70 |
A | THR71 |
A | ASN81 |
A | LEU244 |
A | GLY245 |
A | GLU260 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue ACE A 502 |
Chain | Residue |
A | LEU244 |
A | GLY245 |
A | NAD501 |
A | HOH602 |
B | MET211 |
site_id | AC3 |
Number of Residues | 13 |
Details | binding site for residue CIT A 503 |
Chain | Residue |
A | THR71 |
A | SER79 |
A | ASN81 |
A | ARG85 |
A | ARG95 |
A | ARG116 |
A | TYR123 |
A | ASP231 |
A | NAD501 |
A | HOH619 |
B | LYS174 |
B | ASN176 |
B | ILE177 |
site_id | AC4 |
Number of Residues | 5 |
Details | binding site for residue ACT A 504 |
Chain | Residue |
A | LYS168 |
A | THR170 |
A | ASP202 |
A | ARG204 |
A | PHE220 |
site_id | AC5 |
Number of Residues | 5 |
Details | binding site for residue ACE A 505 |
Chain | Residue |
A | VAL214 |
A | HOH717 |
B | ALA106 |
B | HOH544 |
B | HOH549 |
site_id | AC6 |
Number of Residues | 24 |
Details | binding site for residue NAD B 401 |
Chain | Residue |
A | ASN176 |
A | ILE205 |
A | HOH649 |
B | ILE12 |
B | LYS66 |
B | PRO68 |
B | LEU69 |
B | THR70 |
B | THR71 |
B | ASN81 |
B | GLY245 |
B | GLU260 |
B | VAL262 |
B | HIS263 |
B | GLY264 |
B | SER265 |
B | ALA266 |
B | ASP268 |
B | ALA275 |
B | ASN276 |
B | CIT406 |
B | HOH525 |
B | HOH582 |
B | HOH645 |
site_id | AC7 |
Number of Residues | 6 |
Details | binding site for residue ACE B 402 |
Chain | Residue |
A | ILE177 |
B | LEU122 |
B | GLY125 |
B | ILE126 |
B | GLU127 |
B | ILE142 |
site_id | AC8 |
Number of Residues | 2 |
Details | binding site for residue ACE B 403 |
Chain | Residue |
B | GLY102 |
B | GLU309 |
site_id | AC9 |
Number of Residues | 2 |
Details | binding site for residue ACE B 404 |
Chain | Residue |
B | ARG78 |
B | THR83 |
site_id | AD1 |
Number of Residues | 4 |
Details | binding site for residue ACT B 405 |
Chain | Residue |
A | ALA124 |
B | PHE129 |
B | ILE130 |
B | LYS131 |
site_id | AD2 |
Number of Residues | 13 |
Details | binding site for residue CIT B 406 |
Chain | Residue |
B | ASN81 |
B | ARG85 |
B | ARG95 |
B | ARG116 |
B | TYR123 |
B | ASP231 |
B | NAD401 |
B | HOH554 |
A | LYS174 |
A | ASN176 |
A | HOH690 |
B | THR71 |
B | SER79 |
Functional Information from PROSITE/UniProt
site_id | PS00470 |
Number of Residues | 20 |
Details | IDH_IMDH Isocitrate and isopropylmalate dehydrogenases signature. NLFGDIlSDlaAgli.GGLGL |
Chain | Residue | Details |
A | ASN227-LEU246 |