Research workbench
Crystals structure of classical swine fever virus NS5B (residues 1- 672, Y471A-E472A mutant)
Analyse Crystals structure of classical swine fever virus NS5B (residues 1- 672… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5YF8
- Type
- protein
- Length
- 645 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Rdrp catalytic
- UniProt
- Q5U8X5
- Pockets
- 5 · best druggability 0.84
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Rdrp catalytic | protein | 645 | 44% helix, 13% strand | Q5U8X5 |
Ligands and binding sites
- ACT · Acetate ion · additive · 7 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1111 | 0.84 | 0.85 | 100 | ACT |
| 2 | 79 | 0.65 | 0.92 | 21 | empty |
| 3 | 78 | 0.40 | 0.78 | 18 | ACT |
| 4 | 88 | 0.39 | 0.77 | 22 | empty |
| 5 | 51 | 0.31 | 0.77 | 12 | empty |
Compared structures
- 5YF8 · Crystals structure of Classical swine fever virus NS5B (residues 1-672, Y471A-E472A… · 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 Q5U8X5
- Elsewhere: RCSB PDB 5YF8 · PDBe 5YF8 · UniProt Q5U8X5
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