Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004748 | molecular_function | ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor |
| A | 0005971 | cellular_component | ribonucleoside-diphosphate reductase complex |
| A | 0009263 | biological_process | deoxyribonucleotide biosynthetic process |
| A | 0016020 | cellular_component | membrane |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0004748 | molecular_function | ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor |
| B | 0005971 | cellular_component | ribonucleoside-diphosphate reductase complex |
| B | 0009263 | biological_process | deoxyribonucleotide biosynthetic process |
| B | 0016020 | cellular_component | membrane |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FE2 A 1323 |
| Chain | Residue |
| A | ASP62 |
| A | GLU93 |
| A | HIS96 |
| A | GLU195 |
| A | HOH2015 |
| A | HOH2016 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE2 A 1324 |
| Chain | Residue |
| A | HIS198 |
| A | HOH2016 |
| A | GLU93 |
| A | GLU161 |
| A | GLU195 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FE2 B 1323 |
| Chain | Residue |
| B | ASP62 |
| B | GLU93 |
| B | HIS96 |
| B | GLU195 |
| B | HOH2010 |
| B | HOH2011 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE2 B 1324 |
| Chain | Residue |
| B | GLU93 |
| B | GLU161 |
| B | GLU195 |
| B | HIS198 |
| B | HOH2011 |
Functional Information from PROSITE/UniProt
| site_id | PS00368 |
| Number of Residues | 17 |
| Details | RIBORED_SMALL Ribonucleotide reductase small subunit signature. MEe.VHAkSYshIfttLA |
| Chain | Residue | Details |
| A | MET92-ALA108 | |
