Research workbench
Adenovirus fibre shaft sequence N-terminally fused to the bacteriophage T4 fibritin foldon trimerisation motif with a long 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
- 1V1I
- Type
- protein
- Length
- 300 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fibritin, fiber protein
- UniProt
- P03275, P10104
Structure
x-ray diffraction · 3 distinct chains · 5% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fibritin, fiber protein | protein | 102 | 7% helix, 39% strand | P03275, P10104 |
| B | Fibritin, fiber protein | protein | 100 | 6% helix, 38% strand | P03275, P10104 |
| C | Fibritin, fiber protein | protein | 98 | 3% helix, 38% strand | P03275, P10104 |
Interfaces
3 interfaces between chains.
- A–C · 1930 Ų buried · 30 hydrogen bonds · protein-protein
- A–B · 1916 Ų buried · 31 hydrogen bonds · protein-protein
- B–C · 1854 Ų buried · 31 hydrogen bonds · protein-protein
Compared structures
- 1V1I · 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 1V1I · PDBe 1V1I · UniProt P03275 · UniProt P10104
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