Research workbench
Solution structure of the globular domain of linker histone homolog HHO1P from S. cerevisiae
Analyse Solution structure of the globular domain of linker histone homolog HHO1P from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1UHM
- Type
- protein
- Length
- 78 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 · 47% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histone H1 | protein | 78 | 47% helix, 10% strand | P53551 |
Compared structures
- 1UHM · Solution structure of the globular domain of linker histone homolog Hho1p from S.… · 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 0.79
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 1UHM · PDBe 1UHM · UniProt P53551
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