1UZR
Crystal Structure of the Class Ib Ribonucleotide Reductase R2F-2 subunit from Mycobacterium tuberculosis
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 | 0005971 | cellular_component | ribonucleoside-diphosphate reductase complex |
| A | 0006260 | biological_process | DNA replication |
| 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 | 0005515 | molecular_function | protein binding |
| B | 0005971 | cellular_component | ribonucleoside-diphosphate reductase complex |
| B | 0006260 | biological_process | DNA replication |
| 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 | 0005515 | molecular_function | protein binding |
| C | 0005971 | cellular_component | ribonucleoside-diphosphate reductase complex |
| C | 0006260 | biological_process | DNA replication |
| C | 0009263 | biological_process | deoxyribonucleotide biosynthetic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FE A1292 |
| Chain | Residue |
| A | ASP72 |
| A | GLU103 |
| A | HIS106 |
| A | GLU197 |
| A | FE1293 |
| A | HOH2060 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FE A1293 |
| Chain | Residue |
| A | HIS200 |
| A | FE1292 |
| A | HOH2060 |
| A | GLU103 |
| A | GLU163 |
| A | GLU197 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE B1297 |
| Chain | Residue |
| B | ASP72 |
| B | GLU103 |
| B | HIS106 |
| B | GLU197 |
| B | FE1298 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FE B1298 |
| Chain | Residue |
| B | GLU103 |
| B | GLU163 |
| B | GLU197 |
| B | HIS200 |
| B | FE1297 |
| B | HOH2050 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE C1292 |
| Chain | Residue |
| C | ASP72 |
| C | GLU103 |
| C | HIS106 |
| C | GLU197 |
| C | FE1293 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FE C1293 |
| Chain | Residue |
| C | GLU103 |
| C | GLU163 |
| C | GLU197 |
| C | HIS200 |
| C | FE1292 |
| C | HOH2077 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CIT A1294 |
| Chain | Residue |
| A | GLU151 |
| A | PRO152 |
| A | LEU153 |
| A | LYS154 |
| A | LEU223 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CIT B1299 |
| Chain | Residue |
| B | GLU151 |
| B | PRO152 |
| B | LEU153 |
| B | LYS154 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CIT C1294 |
| Chain | Residue |
| C | GLU151 |
| C | PRO152 |
| C | LEU153 |
| C | LYS154 |
| C | THR219 |
| C | LEU223 |
| site_id | BC1 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE GOL A1295 |
| Chain | Residue |
| A | ARG63 |
| site_id | BC2 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE GOL B1300 |
| Chain | Residue |
| B | ARG63 |
| site_id | BC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL C1295 |
| Chain | Residue |
| C | GLN59 |
| C | ARG63 |
Functional Information from PROSITE/UniProt
| site_id | PS00368 |
| Number of Residues | 17 |
| Details | RIBORED_SMALL Ribonucleotide reductase small subunit signature. MEs.VHAkSYsqIfstLC |
| Chain | Residue | Details |
| A | MET102-CYS118 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | Active site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 15 |
| 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 | TYR110 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1xik |
| Chain | Residue | Details |
| B | TYR110 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1xik |
| Chain | Residue | Details |
| C | TYR110 |
