Research workbench
Engineering the structural stability and functional properties of the gi domain into the intrinsically unfolded gii domain of the yeast linker histone HHO1P
Analyse Engineering the structural stability and functional properties of the gi domain… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1YQA
- Type
- protein
- Length
- 87 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histone H1
- UniProt
- P53551
Structure
solution nmr · 1 distinct chain · 49% helix, 7% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histone H1 | protein | 87 | 49% helix, 7% strand | P53551 |
Compared structures
- 1YQA · Engineering the structural stability and functional properties of the GI domain into the… · the same entry in another collection · chain A against A, TM-score 1.00
- P53551 · AlphaFold monomer V2.0 prediction for histone H1 (P53551) · a predicted model of the same protein · chain A against A, TM-score 0.83
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 P53551
- Elsewhere: RCSB PDB 1YQA · PDBe 1YQA · UniProt P53551
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.