1R65
Crystal structure of ferrous soaked Ribonucleotide Reductase R2 subunit (wildtype) at pH 5 from E. coli
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004748 | molecular_function | ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0005971 | cellular_component | ribonucleoside-diphosphate reductase complex |
| A | 0009185 | biological_process | ribonucleoside diphosphate metabolic process |
| A | 0009263 | biological_process | deoxyribonucleotide biosynthetic process |
| A | 0009265 | biological_process | 2'-deoxyribonucleotide biosynthetic process |
| A | 0015949 | biological_process | nucleobase-containing small molecule interconversion |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0004748 | molecular_function | ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor |
| B | 0005506 | molecular_function | iron ion binding |
| B | 0005515 | molecular_function | protein binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0005971 | cellular_component | ribonucleoside-diphosphate reductase complex |
| B | 0009185 | biological_process | ribonucleoside diphosphate metabolic process |
| B | 0009263 | biological_process | deoxyribonucleotide biosynthetic process |
| B | 0009265 | biological_process | 2'-deoxyribonucleotide biosynthetic process |
| B | 0015949 | biological_process | nucleobase-containing small molecule interconversion |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE2 A 801 |
| Chain | Residue |
| A | ASP84 |
| A | GLU115 |
| A | HIS118 |
| A | PHE208 |
| A | GLU238 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE2 A 802 |
| Chain | Residue |
| A | HIS241 |
| A | TRP111 |
| A | GLU115 |
| A | GLU204 |
| A | GLU238 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE2 B 803 |
| Chain | Residue |
| B | ASP84 |
| B | GLU115 |
| B | HIS118 |
| B | PHE208 |
| B | GLU238 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FE2 B 804 |
| Chain | Residue |
| B | GLU115 |
| B | GLU204 |
| B | GLU238 |
| B | HIS241 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE HG A 901 |
| Chain | Residue |
| A | TYR194 |
| A | MET198 |
| A | ALA265 |
| A | CYS272 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE HG A 902 |
| Chain | Residue |
| A | TYR157 |
| A | CYS196 |
| A | HG910 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE HG A 903 |
| Chain | Residue |
| A | VAL210 |
| A | ALA213 |
| A | CYS214 |
| A | HG911 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE HG B 904 |
| Chain | Residue |
| B | TYR156 |
| B | TYR157 |
| B | CYS196 |
| B | VAL200 |
| B | HG912 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE HG B 905 |
| Chain | Residue |
| B | TYR194 |
| B | LEU195 |
| B | CYS268 |
| B | CYS272 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE HG B 906 |
| Chain | Residue |
| B | VAL210 |
| B | ALA213 |
| B | CYS214 |
| B | LEU304 |
| B | HG914 |
| site_id | BC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE HG A 907 |
| Chain | Residue |
| A | CYS305 |
| A | GLU309 |
| site_id | BC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE HG B 908 |
| Chain | Residue |
| B | TYR194 |
| B | ALA265 |
| B | CYS272 |
| site_id | BC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE HG A 910 |
| Chain | Residue |
| A | TYR157 |
| A | CYS196 |
| A | VAL200 |
| A | HG902 |
| site_id | BC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE HG A 911 |
| Chain | Residue |
| A | ASN76 |
| A | VAL210 |
| A | CYS214 |
| A | LEU290 |
| A | HG903 |
| site_id | BC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE HG B 912 |
| Chain | Residue |
| B | TYR157 |
| B | CYS196 |
| B | VAL200 |
| B | HG904 |
| site_id | BC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE HG B 913 |
| Chain | Residue |
| B | CYS305 |
| B | GLN306 |
| B | GLU309 |
| site_id | BC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE HG B 914 |
| Chain | Residue |
| B | ASN76 |
| B | VAL210 |
| B | CYS214 |
| B | LEU290 |
| B | HG906 |
Functional Information from PROSITE/UniProt
| site_id | PS00368 |
| Number of Residues | 17 |
| Details | RIBORED_SMALL Ribonucleotide reductase small subunit signature. SEt.IHSrSYthIirnIV |
| Chain | Residue | Details |
| A | SER114-VAL130 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | Binding site: {} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1xik |
| Chain | Residue | Details |
| A | TYR122 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1xik |
| Chain | Residue | Details |
| B | TYR122 |
| site_id | MCSA1 |
| Number of Residues | 2 |
| Details | M-CSA 918 |
| Chain | Residue | Details |
| A | TYR122 | pi-pi interaction, single electron relay |
| A | ASP237 |
| site_id | MCSA2 |
| Number of Residues | 2 |
| Details | M-CSA 918 |
| Chain | Residue | Details |
| B | TYR122 | pi-pi interaction, single electron relay |
| B | ASP237 |
