Research workbench
Fibritin deletion mutant M (bacteriophage T4)
Analyse Fibritin deletion mutant M (bacteriophage T4) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1AVY
- Type
- protein
- Length
- 190 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fibritin
- UniProt
- P10104
Structure
x-ray diffraction · 3 distinct chains · 52% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fibritin | protein | 68 | 57% helix, 12% strand | P10104 |
| B | Fibritin | protein | 54 | 46% helix, 15% strand | P10104 |
| C | Fibritin | protein | 68 | 51% helix, 12% strand | P10104 |
Interfaces
2 interfaces between chains.
- A–B · 232 Ų buried · 3 hydrogen bonds · protein-protein
- B–C · 188 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 1AVY · Fibritin deletion mutant M (bacteriophage T4) · 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 P10104
- Elsewhere: RCSB PDB 1AVY · PDBe 1AVY · UniProt P10104
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