Research workbench
Adenovirus fibre shaft sequence N-terminally fused to the bacteriophage T4 fibritin foldon trimerisation motif with a short linker
Analyse Adenovirus fibre shaft sequence N-terminally fused to the bacteriophage T4… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1V1H
- Type
- protein
- Length
- 610 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fibritin, fiber protein
- UniProt
- P03275, P10104
- Pockets
- 3 · best druggability 0.47
Structure
x-ray diffraction · 2 distinct chains · 6% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, E | Fibritin, fiber protein | protein | 103 | 6% helix, 37% strand | P03275, P10104 |
| B, C, D, F | Fibritin, fiber protein | protein | 101 | 6% helix, 38% strand | P03275, P10104 |
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 181 | 0.47 | 0.75 | 19 | empty |
| 2 | 167 | 0.44 | 0.75 | 25 | empty |
| 3 | 127 | 0.39 | 0.74 | 22 | empty |
Interfaces
12 interfaces between chains.
- D–F · 1989 Ų buried · 34 hydrogen bonds · protein-protein
- B–C · 1989 Ų buried · 31 hydrogen bonds · protein-protein
- E–F · 1976 Ų buried · 31 hydrogen bonds · protein-protein
- A–C · 1966 Ų buried · 29 hydrogen bonds · protein-protein
- A–B · 1958 Ų buried · 29 hydrogen bonds · protein-protein
Compared structures
- 1V1H · Adenovirus fibre shaft sequence N-terminally fused to the bacteriophage T4 fibritin… · 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 P03275
- Every structure of UniProt P10104
- Elsewhere: RCSB PDB 1V1H · PDBe 1V1H · UniProt P03275 · UniProt P10104
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