1OQU
A protein coordinated tri-nuclear Fe complex formed during soaking of crystals of the ribonucleotide reductase R2F protein from Corynebacterium Ammoniagenes
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 FE 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 FE A 1002 |
| Chain | Residue |
| A | GLU108 |
| A | GLU168 |
| A | GLU202 |
| A | HIS205 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE B 1003 |
| Chain | Residue |
| B | ASP77 |
| B | GLU108 |
| B | HIS111 |
| B | GLU202 |
| B | FE1004 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE B 1004 |
| Chain | Residue |
| B | GLU108 |
| B | GLU168 |
| B | GLU202 |
| B | HIS205 |
| B | FE1003 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FE C 1001 |
| Chain | Residue |
| C | ASP77 |
| C | GLU108 |
| C | HIS111 |
| C | GLU202 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FE C 1002 |
| Chain | Residue |
| C | GLU108 |
| C | GLU168 |
| C | GLU202 |
| C | HIS205 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE D 1003 |
| Chain | Residue |
| D | ASP77 |
| D | GLU108 |
| D | HIS111 |
| D | PHE172 |
| D | GLU202 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FE D 1004 |
| Chain | Residue |
| D | GLU108 |
| D | GLU168 |
| D | GLU202 |
| D | HIS205 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FE A 2001 |
| Chain | Residue |
| A | GLU245 |
| A | GLU248 |
| A | FE2002 |
| A | FE2003 |
| A | OXY2004 |
| A | HOH2063 |
| A | HOH2200 |
| site_id | BC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FE A 2002 |
| Chain | Residue |
| A | GLU248 |
| A | FE2001 |
| A | FE2003 |
| A | OXY2004 |
| A | HOH2121 |
| A | HOH2192 |
| A | HOH2201 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FE A 2003 |
| Chain | Residue |
| A | GLU245 |
| A | FE2001 |
| A | FE2002 |
| A | OXY2004 |
| A | HOH2063 |
| A | HOH2201 |
| site_id | BC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE FE B 1005 |
| Chain | Residue |
| B | GLU248 |
| B | FE1006 |
| B | FE1007 |
| site_id | BC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE FE B 1006 |
| Chain | Residue |
| B | GLU248 |
| B | FE1005 |
| site_id | BC5 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE FE B 1007 |
| Chain | Residue |
| B | FE1005 |
| site_id | BC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE FE C 1008 |
| Chain | Residue |
| C | GLU245 |
| C | ASP324 |
| C | ASP326 |
| C | ASP328 |
| C | FE1009 |
| C | FE1010 |
| C | OXY1012 |
| C | HOH1214 |
| site_id | BC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE FE C 1009 |
| Chain | Residue |
| C | GLU248 |
| C | ASP326 |
| C | ASP328 |
| C | FE1008 |
| C | FE1010 |
| C | ACT1011 |
| C | OXY1012 |
| C | HOH1154 |
| site_id | BC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE FE C 1010 |
| Chain | Residue |
| C | GLU245 |
| C | GLU248 |
| C | ASP324 |
| C | FE1008 |
| C | FE1009 |
| C | ACT1011 |
| C | OXY1012 |
| C | HOH1188 |
| site_id | BC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FE D 1012 |
| Chain | Residue |
| D | GLU248 |
| D | FE1014 |
| D | OXY1015 |
| D | HOH1033 |
| D | HOH1106 |
| D | HOH1127 |
| site_id | CC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FE D 1013 |
| Chain | Residue |
| D | GLU245 |
| D | GLU248 |
| D | OXY1015 |
| D | HOH1033 |
| site_id | CC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE D 1014 |
| Chain | Residue |
| D | HOH1127 |
| D | HOH1171 |
| D | GLU245 |
| D | FE1012 |
| D | OXY1015 |
| site_id | CC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE ACT C 1011 |
| Chain | Residue |
| C | GLU248 |
| C | ASP324 |
| C | ASP326 |
| C | FE1009 |
| C | FE1010 |
| C | OXY1012 |
| C | HOH1154 |
| C | HOH1163 |
| C | HOH1188 |
| site_id | CC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE OXY A 2004 |
| Chain | Residue |
| A | GLU245 |
| A | GLU248 |
| A | FE2001 |
| A | FE2002 |
| A | FE2003 |
| A | HOH2063 |
| A | HOH2121 |
| A | HOH2201 |
| site_id | CC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE OXY C 1012 |
| Chain | Residue |
| C | GLU245 |
| C | GLU248 |
| C | ASP324 |
| C | ASP326 |
| C | ASP328 |
| C | FE1008 |
| C | FE1009 |
| C | FE1010 |
| C | ACT1011 |
| site_id | CC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE OXY D 1015 |
| Chain | Residue |
| D | GLU245 |
| D | GLU248 |
| D | FE1012 |
| D | FE1013 |
| D | FE1014 |
| D | HOH1033 |
| D | HOH1171 |
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 |
