Research workbench
Structure of vaccinia virus A27
Analyse Structure of vaccinia virus A27 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3VOP
- Type
- protein
- Length
- 123 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein A27
- UniProt
- P11258
Structure
x-ray diffraction · 2 distinct chains · 89% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Protein A27 | protein | 40 | 93% helix, 0% strand | P11258 |
| C | Protein A27 | protein | 43 | 86% helix, 0% strand | P11258 |
Ligands and binding sites
- PEG · Di(hydroxyethyl)ether · additive · 9 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
3 interfaces between chains.
- A–B · 766 Ų buried · 3 hydrogen bonds · protein-protein
- B–C · 495 Ų buried · 0 hydrogen bonds · protein-protein
- A–C · 487 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 3VOP · Structure of Vaccinia virus A27 · 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 P11258
- Elsewhere: RCSB PDB 3VOP · PDBe 3VOP · UniProt P11258
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