Research workbench
Structure of the C-terminal head domain of the fowl adenovirus type 1 short fibre
Analyse Structure of the C-terminal head domain of the fowl adenovirus type 1 short… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2VTW
- Type
- protein
- Length
- 1,230 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fiber protein 2
- UniProt
- Q64762
- Ligands
- SO4
- Pockets
- 12 · best druggability 0.83
Structure
x-ray diffraction · 1 distinct chain · 5% helix, 48% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | Fiber protein 2 | protein | 205 | 5% helix, 48% strand | Q64762 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 10 copies · chains A, B, C, D, E, F
- GOL · Glycerol · additive · 2 copies · chains B, E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 241 | 0.83 | 0.95 | 47 | empty |
| 2 | 243 | 0.83 | 0.95 | 39 | empty |
| 3 | 481 | 0.59 | 0.74 | 64 | empty |
| 4 | 92 | 0.41 | 0.77 | 22 | empty |
| 5 | 103 | 0.39 | 0.76 | 23 | empty |
Interfaces
8 interfaces between chains.
- C–D · 1022 Ų buried · 10 hydrogen bonds · protein-protein
- A–F · 1021 Ų buried · 8 hydrogen bonds · protein-protein
- A–E · 1010 Ų buried · 10 hydrogen bonds · protein-protein
- B–D · 1007 Ų buried · 11 hydrogen bonds · protein-protein
- E–F · 1003 Ų buried · 10 hydrogen bonds · protein-protein
Compared structures
- 2VTW · Structure of the C-terminal head domain of the fowl adenovirus type 1 short fibre · 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 Q64762
- Elsewhere: RCSB PDB 2VTW · PDBe 2VTW · UniProt Q64762
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