Research workbench
Structure of Uranotaenia sapphirina cypovirus (CPV17) polyhedrin at 100 K
Analyse Structure of Uranotaenia sapphirina cypovirus (CPV17) polyhedrin at 100 K in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4S1K
- Type
- protein
- Length
- 236 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.2
- Source
- Uranotaenia sapphirina cypovirus
- Molecule
- Polyhedrin
- UniProt
- Q5EK29
- Ligands
- ATP, MG
- Pockets
- 2 · best druggability 0.36
Structure
x-ray diffraction · resolution 2.2 · 1 distinct chain · 28% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Polyhedrin | protein | 236 | 28% helix, 28% strand | Q5EK29 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 69 | 0.36 | 0.77 | 12 | empty |
| 2 | 72 | 0.32 | 0.74 | 19 | empty |
Compared structures
- 4S1K · Structure of uranotaenia sapphirina cypovirus (CPV17) polyhedrin at 100 K · 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 Q5EK29
- Elsewhere: RCSB PDB 4S1K · PDBe 4S1K · UniProt Q5EK29
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