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Crystal structure of cleavage site mutant of npro of classical swine fever virus.
Analyse Crystal structure of cleavage site mutant of npro of classical swine fever… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4H9K
- Type
- protein
- Length
- 147 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hog cholera virus
- UniProt
- Q68871
- Ligands
- ZN, SO4
- Pockets
- 1 · best druggability 0.31
Structure
x-ray diffraction · 1 distinct chain · 2% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hog cholera virus | protein | 147 | 2% helix, 36% strand | Q68871 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 79 | 0.31 | 0.73 | 16 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 4H9K · Crystal structure of cleavage site mutant of Npro of classical swine fever virus. · 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 Q68871
- Elsewhere: RCSB PDB 4H9K · PDBe 4H9K · UniProt Q68871
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