Research workbench
Canarypox virus resolvase
Analyse Canarypox virus resolvase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5E6F
- Type
- protein
- Length
- 260 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- CNPV261 holliday junction resolvase protein
- UniProt
- Q6VZ86
- Ligands
- MG
- Pockets
- 3 · best druggability 0.41
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | CNPV261 holliday junction resolvase protein | protein | 130 | 38% helix, 24% strand | Q6VZ86 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 98 | 0.41 | 0.77 | 20 | empty |
| 2 | 112 | 0.40 | 0.76 | 23 | MG |
| 3 | 94 | 0.38 | 0.76 | 20 | MG |
Interfaces
1 interface between chains.
- A–B · 705 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 5E6F · Canarypox virus resolvase · 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 Q6VZ86
- Elsewhere: RCSB PDB 5E6F · PDBe 5E6F · UniProt Q6VZ86
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