1XJK
Structural mechanism of allosteric substrate specificity in a ribonucleotide reductase: dGTP-ADP complex
Entity
| Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
| 1 | A, B | ribonucleotide reductase, B12-dependent | polymer | 644 | 73360.2 | 2 | UniProt (O33839) Pfam (PF00317) Pfam (PF02867) In PDB | Thermotoga maritima | |
| 2 | A, B | MAGNESIUM ION | non-polymer | 24.3 | 2 | Chemie (MG) | |||
| 3 | A, B | ADENOSINE-5'-DIPHOSPHATE | non-polymer | 427.2 | 2 | Chemie (ADP) | |||
| 4 | A, B | 2'-DEOXYGUANOSINE-5'-TRIPHOSPHATE | non-polymer | 507.2 | 2 | Chemie (DGT) | |||
| 5 | water | water | 18.0 | 247 | Chemie (HOH) |
Sequence modifications
A, B: 1 - 644 (UniProt: O33839)
| PDB | External Database | Details |
|---|---|---|
| Ser 205 | Tyr 205 | SEE REMARK 999 |
| Asp 519 | Glu 519 | conflict |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 2 |
| Total formula weight | 146720.4 | |
| Non-Polymers* | Number of molecules | 6 |
| Total formula weight | 1917.4 | |
| All* | Total formula weight | 148637.8 |
