1KGN
R2F from Corynebacterium Ammoniagenes in its oxidised, Fe containing, form
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 | 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 | 0016491 | molecular_function | oxidoreductase activity |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0004748 | molecular_function | ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor |
| C | 0005971 | cellular_component | ribonucleoside-diphosphate reductase complex |
| C | 0009263 | biological_process | deoxyribonucleotide biosynthetic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0004748 | molecular_function | ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor |
| D | 0005971 | cellular_component | ribonucleoside-diphosphate reductase complex |
| D | 0009263 | biological_process | deoxyribonucleotide biosynthetic process |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE FE A 1001 |
| Chain | Residue |
| A | ASP77 |
| A | GLU108 |
| A | HIS111 |
| A | GLU202 |
| A | FE2001 |
| A | HOH2096 |
| A | HOH2147 |
| A | HOH2427 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE FE B 1002 |
| Chain | Residue |
| B | GLU108 |
| B | HIS111 |
| B | GLU202 |
| B | FE2002 |
| B | HOH2064 |
| B | HOH2164 |
| B | HOH2364 |
| B | ASP77 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE D 1003 |
| Chain | Residue |
| D | ASP77 |
| D | GLU108 |
| D | HIS111 |
| D | GLU202 |
| D | FE1004 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE D 1004 |
| Chain | Residue |
| D | GLU108 |
| D | GLU168 |
| D | GLU202 |
| D | HIS205 |
| D | FE1003 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FE A 2001 |
| Chain | Residue |
| A | GLU108 |
| A | GLU168 |
| A | GLU202 |
| A | HIS205 |
| A | FE1001 |
| A | HOH2096 |
| A | HOH2427 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FE B 2002 |
| Chain | Residue |
| B | GLU108 |
| B | GLU168 |
| B | GLU202 |
| B | HIS205 |
| B | FE1002 |
| B | HOH2164 |
| B | HOH2364 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE FE C 3001 |
| Chain | Residue |
| C | ASP77 |
| C | GLU108 |
| C | HIS111 |
| C | GLU202 |
| C | FE3002 |
| C | HOH3051 |
| C | HOH3060 |
| C | HOH3403 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FE C 3002 |
| Chain | Residue |
| C | GLU108 |
| C | GLU168 |
| C | GLU202 |
| C | HIS205 |
| C | FE3001 |
| C | HOH3051 |
| C | HOH3403 |
Functional Information from PROSITE/UniProt
| site_id | PS00368 |
| Number of Residues | 17 |
| Details | RIBORED_SMALL Ribonucleotide reductase small subunit signature. MEs.VHAkSYsnIfmtLA |
| Chain | Residue | Details |
| A | MET107-ALA123 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1xik |
| Chain | Residue | Details |
| A | TYR115 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1xik |
| Chain | Residue | Details |
| B | TYR115 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1xik |
| Chain | Residue | Details |
| C | TYR115 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1xik |
| Chain | Residue | Details |
| D | TYR115 |
