Research workbench
Crystal structure of the conserved core domain of VP22 from HSV-1
Analyse Crystal structure of the conserved core domain of VP22 from HSV-1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4XAL
- Type
- protein
- Length
- 96 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tegument protein VP22; Peptide ssgvdl
- UniProt
- P10233
Structure
x-ray diffraction · 2 distinct chains · 56% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tegument protein VP22 | protein | 90 | 60% helix, 4% strand | P10233 |
| B | Peptide ssgvdl | protein | 6 | 0% helix, 67% strand | — |
Interfaces
1 interface between chains.
- A–B · 410 Ų buried · 12 hydrogen bonds · protein-protein
Compared structures
- 4XAL · Crystal structure of the conserved core domain of VP22 from HSV-1 · 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 P10233
- Elsewhere: RCSB PDB 4XAL · PDBe 4XAL · UniProt P10233
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