Research workbench
Azide complex of the diferrous E238A mutant R2 subunit of ribonucleotide reductase
Analyse Azide complex of the diferrous E238A mutant R2 subunit of ribonucleotide… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1RSV
- Type
- protein
- Length
- 681 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ribonucleoside-diphosphate reductase 1 beta chain
- EC
- 1.17.4.1
- UniProt
- P69924
- Ligands
- HG, FE, AZI
- Pockets
- 1 · best druggability 0.74
Structure
x-ray diffraction · 2 distinct chains · 69% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ribonucleoside-diphosphate reductase 1 beta chain (EC 1.17.4.1) | protein | 340 | 71% helix, 4% strand | P69924 |
| B | Ribonucleoside-diphosphate reductase 1 beta chain (EC 1.17.4.1) | protein | 341 | 68% helix, 4% strand | P69924 |
Ligands and binding sites
- HG · Mercury (II) ion · metal · 12 copies · chains A, B
- FE · Fe (III) ion · metal · 4 copies · chains A, B
- AZI · Azide ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 117 | 0.74 | 0.94 | 26 | empty |
Interfaces
1 interface between chains.
- A–B · 3097 Ų buried · 52 hydrogen bonds · protein-protein
Compared structures
- 1RSV · azide complex of the diferrous E238A mutant R2 subunit of ribonucleotide reductase · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P69924
- Elsewhere: RCSB PDB 1RSV · PDBe 1RSV · UniProt P69924
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