1RNR
AUTOCATALYTIC GENERATION OF DOPA IN THE ENGINEERED PROTEIN R2 F208Y FROM ESCHERICHIA COLI RIBONUCLEOTIDE REDUCTASE AND CRYSTAL STRUCTURE OF THE DOPA-208 PROTEIN
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 | 6 |
| Details | BINDING SITE FOR RESIDUE FE A 401 |
| Chain | Residue |
| A | FE402 |
| A | ASP84 |
| A | GLU115 |
| A | HIS118 |
| A | DAH208 |
| A | GLU238 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FE A 402 |
| Chain | Residue |
| A | GLU115 |
| A | GLU204 |
| A | DAH208 |
| A | GLU238 |
| A | HIS241 |
| A | FE401 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE HG A 403 |
| Chain | Residue |
| A | TYR156 |
| A | TYR157 |
| A | CYS196 |
| A | HG406 |
| A | HOH417 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE HG A 404 |
| Chain | Residue |
| A | TYR194 |
| A | CYS272 |
| A | HG407 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE HG A 405 |
| Chain | Residue |
| A | VAL210 |
| A | CYS214 |
| A | HOH414 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE HG A 406 |
| Chain | Residue |
| A | LEU95 |
| A | TYR157 |
| A | CYS196 |
| A | VAL200 |
| A | HG403 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE HG A 407 |
| Chain | Residue |
| A | TYR194 |
| A | CYS268 |
| A | CYS272 |
| A | HG404 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE HG A 408 |
| Chain | Residue |
| A | CYS305 |
| A | GLN306 |
| A | GLU309 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FE B 401 |
| Chain | Residue |
| B | ASP84 |
| B | GLU115 |
| B | HIS118 |
| B | DAH208 |
| B | GLU238 |
| B | FE402 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FE B 402 |
| Chain | Residue |
| B | GLU115 |
| B | GLU204 |
| B | DAH208 |
| B | GLU238 |
| B | HIS241 |
| B | FE401 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE HG B 403 |
| Chain | Residue |
| B | TYR156 |
| B | TYR157 |
| B | CYS196 |
| B | HG408 |
| B | HOH421 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE HG B 404 |
| Chain | Residue |
| B | VAL210 |
| B | ALA213 |
| B | CYS214 |
| B | LEU304 |
| B | HG407 |
| site_id | BC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE HG B 405 |
| Chain | Residue |
| B | TYR194 |
| B | MET198 |
| B | CYS272 |
| B | HOH413 |
| site_id | BC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE HG B 406 |
| Chain | Residue |
| B | MET198 |
| B | CYS272 |
| B | PHE276 |
| site_id | BC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE HG B 407 |
| Chain | Residue |
| B | VAL210 |
| B | CYS214 |
| B | LEU290 |
| B | HG404 |
| site_id | BC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE HG B 408 |
| Chain | Residue |
| B | TYR157 |
| B | CYS196 |
| B | VAL200 |
| B | HG403 |
| B | HOH412 |
| site_id | BC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE HG B 409 |
| Chain | Residue |
| B | TYR194 |
| B | LEU195 |
| B | CYS268 |
| B | CYS272 |
| site_id | BC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE HG B 410 |
| Chain | Residue |
| B | PHE73 |
| B | ASN76 |
| B | SER215 |
| site_id | FEA |
| Number of Residues | 2 |
| Details |
| Chain | Residue |
| A | FE401 |
| A | FE402 |
| site_id | FEB |
| Number of Residues | 2 |
| Details |
| Chain | Residue |
| B | HG403 |
| B | HG404 |
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 | ACT_SITE: |
| Chain | Residue | Details |
| A | THR123 | |
| B | THR123 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | SER85 | |
| A | ALA239 | |
| A | LEU242 | |
| B | SER85 | |
| B | THR116 | |
| B | SER119 | |
| B | ALA205 | |
| B | ALA239 | |
| B | LEU242 | |
| A | THR116 | |
| A | SER119 | |
| A | ALA205 |
