Research workbench
Crystal structure of NSP15-H234A mutant- hexamer in asymmetric unit
Analyse Crystal structure of NSP15-H234A mutant- hexamer in asymmetric unit in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2RHB
- Type
- protein
- Length
- 2,072 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Uridylate-specific endoribonuclease
- UniProt
- P59641
- Pockets
- 20 · best druggability 0.82
Structure
x-ray diffraction · 3 distinct chains · 21% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Uridylate-specific endoribonuclease | protein | 345 | 21% helix, 31% strand | P59641 |
| B, D, E | Uridylate-specific endoribonuclease | protein | 346 | 21% helix, 31% strand | P59641 |
| F | Uridylate-specific endoribonuclease | protein | 344 | 20% helix, 31% strand | P59641 |
Pockets
20 pockets found on a 1 Å grid, 15 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 976 | 0.82 | 0.84 | 88 | empty |
| 2 | 851 | 0.78 | 0.81 | 83 | empty |
| 3 | 382 | 0.76 | 0.86 | 50 | empty |
| 4 | 896 | 0.76 | 0.79 | 71 | empty |
| 5 | 64 | 0.73 | 0.98 | 19 | empty |
Interfaces
13 interfaces between chains.
- E–F · 1225 Ų buried · 13 hydrogen bonds · protein-protein
- D–F · 1196 Ų buried · 11 hydrogen bonds · protein-protein
- B–C · 1181 Ų buried · 12 hydrogen bonds · protein-protein
- A–C · 1181 Ų buried · 16 hydrogen bonds · protein-protein
- D–E · 1172 Ų buried · 12 hydrogen bonds · protein-protein
Compared structures
- 2RHB · Crystal structure of Nsp15-H234A mutant- Hexamer in asymmetric unit · 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 P59641
- Elsewhere: RCSB PDB 2RHB · PDBe 2RHB · UniProt P59641
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