6RQA
Crystal structure of the iminosuccinate reductase of Paracoccus denitrificans in complex with NAD+
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0009436 | biological_process | glyoxylate catabolic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016639 | molecular_function | oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor |
| A | 0046296 | biological_process | glycolate catabolic process |
| A | 0070404 | molecular_function | NADH binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0009436 | biological_process | glyoxylate catabolic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016639 | molecular_function | oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor |
| B | 0046296 | biological_process | glycolate catabolic process |
| B | 0070404 | molecular_function | NADH binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 22 |
| Details | binding site for residue NAD A 401 |
| Chain | Residue |
| A | HIS83 |
| A | MET164 |
| A | ILE197 |
| A | THR198 |
| A | SER199 |
| A | SER200 |
| A | MET219 |
| A | GLY220 |
| A | ASP222 |
| A | LYS226 |
| A | GLY291 |
| A | ARG110 |
| A | THR292 |
| A | GLY293 |
| A | HOH514 |
| A | THR111 |
| A | GLY136 |
| A | HIS137 |
| A | GLN138 |
| A | ASN159 |
| A | PRO160 |
| A | HIS161 |
| site_id | AC2 |
| Number of Residues | 1 |
| Details | binding site for residue TB A 402 |
| Chain | Residue |
| A | ASP48 |
| site_id | AC3 |
| Number of Residues | 1 |
| Details | binding site for residue TB A 403 |
| Chain | Residue |
| A | GLU163 |
| site_id | AC4 |
| Number of Residues | 22 |
| Details | binding site for residue NAD B 401 |
| Chain | Residue |
| B | ARG110 |
| B | THR111 |
| B | GLY134 |
| B | ALA135 |
| B | GLY136 |
| B | HIS137 |
| B | GLN138 |
| B | ASN159 |
| B | PRO160 |
| B | HIS161 |
| B | ILE197 |
| B | THR198 |
| B | SER199 |
| B | SER200 |
| B | MET219 |
| B | GLY220 |
| B | ASP222 |
| B | LYS226 |
| B | GLY291 |
| B | THR292 |
| B | GLY293 |
| B | HOH525 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue 7MT B 402 |
| Chain | Residue |
| A | ASN79 |
| A | LEU80 |
| B | GLU47 |
| B | ASP48 |
| B | ASN74 |
| B | HOH527 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor/acceptor => ECO:0000250|UniProtKB:O28608 |
| Chain | Residue | Details |
| A | LYS67 | |
| B | LYS67 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 14 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:31723261 |
| Chain | Residue | Details |
| A | ARG110 | |
| B | ASN159 | |
| B | SER199 | |
| B | MET219 | |
| B | LYS226 | |
| B | GLY291 | |
| A | HIS137 | |
| A | ASN159 | |
| A | SER199 | |
| A | MET219 | |
| A | LYS226 | |
| A | GLY291 | |
| B | ARG110 | |
| B | HIS137 |
