MolNFT v1 · #28832 · protein
Engineering the structural stability and functional properties of the gi domain into the intrinsically unfolded gii domain of the yeast linker histone HHO1P
1YQA · Histone H1: “Engineering the structural stability and functional properties of the gi domain into the intrinsically…”. Solution nmr. MolNFT v1 #28832 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- 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
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