Research workbench
Molecular dynamics flexible fitting model of coxsackievirus A16 empty procapsid VP1 subunit
Analyse Molecular dynamics flexible fitting model of coxsackievirus A16 empty procapsid… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5TSK
- Type
- protein
- Length
- 219 residues
- Chains
- 1
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Coxsackievirus A16 empty procapsid VP1 subunit
- Pockets
- 2 · best druggability 0.64
Structure
electron microscopy · 1 distinct chain · 10% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Coxsackievirus A16 empty procapsid VP1 subunit | protein | 219 | 10% helix, 32% strand | — |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 333 | 0.64 | 0.80 | 38 | empty |
| 2 | 91 | 0.44 | 0.79 | 18 | empty |
Compared structures
- 5TSK · Molecular Dynamics Flexible Fitting Model of Coxsackievirus A16 empty Procapsid VP1… · 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
- Elsewhere: RCSB PDB 5TSK · PDBe 5TSK
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