Research workbench
Inovirus (filamentous bacteriophage) strain PF1 major coat protein assembly
Analyse Inovirus (filamentous bacteriophage) strain PF1 major coat protein assembly in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1QL2
- Type
- protein
- Length
- 138 residues
- Chains
- 3
- Method
- fiber diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- PF1 bacteriophage coat protein B
- UniProt
- P03621
Structure
fiber diffraction · 1 distinct chain · 87% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | PF1 bacteriophage coat protein B | protein | 46 | 87% helix, 0% strand | P03621 |
Interfaces
2 interfaces between chains.
- A–B · 57 Ų buried · 0 hydrogen bonds · protein-protein
- B–C · 50 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 1QL2 · Inovirus (Filamentous Bacteriophage) Strain PF1 Major Coat Protein Assembly · 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 P03621
- Elsewhere: RCSB PDB 1QL2 · PDBe 1QL2 · UniProt P03621
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