Research workbench
Novel dimerization motif in the dead box RNA helicase hera: form 1, partial dimer
Analyse Novel dimerization motif in the dead box RNA helicase hera: form 1, partial… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3EAR
- Type
- protein
- Length
- 256 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hera
- UniProt
- Q72GF3
Structure
x-ray diffraction · 2 distinct chains · 57% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hera | protein | 206 | 51% helix, 16% strand | Q72GF3 |
| B | Hera | protein | 50 | 78% helix, 0% strand | Q72GF3 |
Interfaces
1 interface between chains.
- A–B · 1585 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 3EAR · Novel dimerization motif in the DEAD box RNA helicase Hera: form 1, partial dimer · 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 Q72GF3
- Elsewhere: RCSB PDB 3EAR · PDBe 3EAR · UniProt Q72GF3
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