1KGP
R2F from Corynebacterium Ammoniagenes in its Mn substituted 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 | 5 | 
| Details | BINDING SITE FOR RESIDUE MN A 1001 | 
| Chain | Residue | 
| A | ASP77 | 
| A | GLU108 | 
| A | HIS111 | 
| A | PHE172 | 
| A | GLU202 | 
| site_id | AC2 | 
| Number of Residues | 4 | 
| Details | BINDING SITE FOR RESIDUE MN A 1002 | 
| Chain | Residue | 
| A | GLU108 | 
| A | GLU168 | 
| A | GLU202 | 
| A | HIS205 | 
| site_id | AC3 | 
| Number of Residues | 5 | 
| Details | BINDING SITE FOR RESIDUE MN B 1003 | 
| Chain | Residue | 
| B | ASP77 | 
| B | GLU108 | 
| B | HIS111 | 
| B | PHE172 | 
| B | GLU202 | 
| site_id | AC4 | 
| Number of Residues | 4 | 
| Details | BINDING SITE FOR RESIDUE MN B 1004 | 
| Chain | Residue | 
| B | GLU108 | 
| B | GLU168 | 
| B | GLU202 | 
| B | HIS205 | 
| site_id | AC5 | 
| Number of Residues | 4 | 
| Details | BINDING SITE FOR RESIDUE MN C 2001 | 
| Chain | Residue | 
| C | ASP77 | 
| C | GLU108 | 
| C | HIS111 | 
| C | GLU202 | 
| site_id | AC6 | 
| Number of Residues | 4 | 
| Details | BINDING SITE FOR RESIDUE MN C 2002 | 
| Chain | Residue | 
| C | GLU108 | 
| C | GLU168 | 
| C | GLU202 | 
| C | HIS205 | 
| site_id | AC7 | 
| Number of Residues | 5 | 
| Details | BINDING SITE FOR RESIDUE MN D 2003 | 
| Chain | Residue | 
| D | ASP77 | 
| D | GLU108 | 
| D | HIS111 | 
| D | PHE172 | 
| D | GLU202 | 
| site_id | AC8 | 
| Number of Residues | 4 | 
| Details | BINDING SITE FOR RESIDUE MN D 2004 | 
| Chain | Residue | 
| D | GLU108 | 
| D | GLU168 | 
| D | GLU202 | 
| D | HIS205 | 
| site_id | AC9 | 
| Number of Residues | 5 | 
| Details | BINDING SITE FOR RESIDUE MN C 3001 | 
| Chain | Residue | 
| C | HOH3073 | 
| C | HOH3147 | 
| C | HOH3174 | 
| D | HOH2037 | 
| D | HOH2064 | 
| site_id | BC1 | 
| Number of Residues | 2 | 
| Details | BINDING SITE FOR RESIDUE MN C 3002 | 
| Chain | Residue | 
| C | GLU222 | 
| C | GLU226 | 
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 | 






