Research workbench
Structural basis for the enhancement of virulence by entomopoxvirus fusolin and its in vivo crystallization into viral spindles
Analyse Structural basis for the enhancement of virulence by entomopoxvirus fusolin and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4OW5
- Type
- protein
- Length
- 307 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fusolin
- UniProt
- Q83389
Structure
x-ray diffraction · 1 distinct chain · 27% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fusolin | protein | 307 | 27% helix, 24% strand | Q83389 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · 7 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
- 4OW5 · Structural basis for the enhancement of virulence by entomopoxvirus fusolin and its in… · 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 Q83389
- Elsewhere: RCSB PDB 4OW5 · PDBe 4OW5 · UniProt Q83389
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