1W69
Crystal Structure of Mouse Ribonucleotide Reductase Subunit R2 under Reducing Conditions. A Fully Occupied Dinuclear Iron Cluster and Bound Acetate.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004748 | molecular_function | ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor |
| A | 0005515 | molecular_function | protein binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005635 | cellular_component | nuclear envelope |
| A | 0005654 | cellular_component | nucleoplasm |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0005971 | cellular_component | ribonucleoside-diphosphate reductase complex |
| A | 0006281 | biological_process | DNA repair |
| A | 0008199 | molecular_function | ferric iron binding |
| A | 0008284 | biological_process | positive regulation of cell population proliferation |
| A | 0009185 | biological_process | ribonucleoside diphosphate metabolic process |
| A | 0009262 | biological_process | deoxyribonucleotide metabolic process |
| A | 0009263 | biological_process | deoxyribonucleotide biosynthetic process |
| A | 0009265 | biological_process | 2'-deoxyribonucleotide biosynthetic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0036175 | molecular_function | ribonucleoside-diphosphate reductase activity, glutaredoxin disulfide as acceptor |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051290 | biological_process | protein heterotetramerization |
| A | 1900087 | biological_process | positive regulation of G1/S transition of mitotic cell cycle |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FE2 A1349 |
| Chain | Residue |
| A | ASP139 |
| A | GLU170 |
| A | HIS173 |
| A | GLU267 |
| A | FE21350 |
| A | ACY1351 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FE2 A1350 |
| Chain | Residue |
| A | HIS270 |
| A | FE21349 |
| A | ACY1351 |
| A | GLU170 |
| A | GLU233 |
| A | GLU267 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE ACY A1351 |
| Chain | Residue |
| A | ASP139 |
| A | VAL142 |
| A | GLU170 |
| A | GLU233 |
| A | GLU267 |
| A | FE21349 |
| A | FE21350 |
Functional Information from PROSITE/UniProt
| site_id | PS00368 |
| Number of Residues | 17 |
| Details | RIBORED_SMALL Ribonucleotide reductase small subunit signature. MEn.IHSeMYslLidtYI |
| Chain | Residue | Details |
| A | MET169-ILE185 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10014","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| 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 | TYR177 |
