Research workbench
The cryo-EM structure of hev vlp
Analyse The cryo-EM structure of hev vlp in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6LAT
- Type
- protein
- Length
- 458 residues
- Chains
- 1
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein ORF2
- UniProt
- A0A4P6DD72
- Pockets
- 3 · best druggability 0.71
Structure
electron microscopy · 1 distinct chain · 5% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein ORF2 | protein | 458 | 5% helix, 35% strand | A0A4P6DD72 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 59 | 0.71 | 0.98 | 26 | empty |
| 2 | 108 | 0.43 | 0.77 | 20 | empty |
| 3 | 51 | 0.31 | 0.77 | 16 | empty |
Compared structures
- 6LAT · The cryo-EM structure of HEV VLP · 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 A0A4P6DD72
- Elsewhere: RCSB PDB 6LAT · PDBe 6LAT · UniProt A0A4P6DD72
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