1H7A
Structural basis for allosteric substrate specificity regulation in class III ribonucleotide reductases: NRDD in complex with dATP
Replaces: 1B8BEntity
| Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
| 1 | A | ANAEROBIC RIBONUCLEOTIDE-TRIPHOSPHATE REDUCTASE LARGE CHAIN | polymer | 605 | 68055.6 | 1 | UniProt (Q9T0V5) Pfam (PF01228) UniProt (by SIFTS) (P07071) In PDB | BACTERIOPHAGE T4 | ANAEROBIC NTP REDUCTASE |
| 2 | A | 2'-DEOXYADENOSINE 5'-TRIPHOSPHATE | non-polymer | 491.2 | 1 | Chemie (DTP) | |||
| 3 | A | FE (II) ION | non-polymer | 55.8 | 1 | Chemie (FE2) | |||
| 4 | A | MAGNESIUM ION | non-polymer | 24.3 | 1 | Chemie (MG) | |||
| 5 | water | water | 18.0 | 58 | Chemie (HOH) |
Sequence modifications
A: 1 - 605 (UniProt: Q9T0V5)
| PDB | External Database | Details |
|---|---|---|
| Ala 580 | Gly 580 | engineered mutation |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 1 |
| Total formula weight | 68055.6 | |
| Non-Polymers* | Number of molecules | 3 |
| Total formula weight | 571.3 | |
| All* | Total formula weight | 68626.9 |
