Research workbench
Crystal structure of dettilon tailspike protein (GP208)
Analyse Crystal structure of dettilon tailspike protein (GP208) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6F7D
- Type
- protein
- Length
- 538 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tailspike
- UniProt
- A0A0C5PVE3
- Pockets
- 1 · best druggability 0.57
Structure
x-ray diffraction · 1 distinct chain · 7% helix, 45% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tailspike | protein | 538 | 7% helix, 45% strand | A0A0C5PVE3 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · 2 copies · 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 | 289 | 0.57 | 0.77 | 35 | EDO |
Compared structures
- 6F7D · Crystal structure of Dettilon tailspike protein (gp208) · 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 A0A0C5PVE3
- Elsewhere: RCSB PDB 6F7D · PDBe 6F7D · UniProt A0A0C5PVE3
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