Research workbench
Dimeric structure of the C-terminal domain of vpr
Analyse Dimeric structure of the C-terminal domain of vpr in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1X9V
- Type
- protein
- Length
- 90 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Vpr protein
- UniProt
- Q73369
Structure
solution nmr · 1 distinct chain · 47% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Vpr protein | protein | 45 | 47% helix, 0% strand | Q73369 |
Interfaces
1 interface between chains.
- A–B · 473 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 1X9V · Dimeric structure of the C-terminal domain of Vpr · 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 Q73369
- Elsewhere: RCSB PDB 1X9V · PDBe 1X9V · UniProt Q73369
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