Research workbench
Bacteriophage PHI812K1-420 major capsid protein
Analyse Bacteriophage PHI812K1-420 major capsid protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5LII
- Type
- protein
- Length
- 433 residues
- Chains
- 1
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Major capsid protein
- UniProt
- A1YTN4
- Pockets
- 3 · best druggability 0.72
Structure
electron microscopy · 1 distinct chain · 10% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| P | Major capsid protein | protein | 433 | 10% helix, 10% strand | A1YTN4 |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 713 | 0.72 | 0.78 | 82 | empty |
| 2 | 181 | 0.66 | 0.86 | 34 | empty |
| 3 | 53 | 0.26 | 0.73 | 14 | empty |
Compared structures
- 5LII · bacteriophage phi812K1-420 major capsid protein · the same entry in another collection · chain P against P, 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 A1YTN4
- Elsewhere: RCSB PDB 5LII · PDBe 5LII · UniProt A1YTN4
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