Research workbench
Solution NMR structure of the globular domain of human histone H1X, northeast structural genomics consortium (nesg) target HR7057A
Analyse Solution NMR structure of the globular domain of human histone H1X, northeast… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2LSO
- Type
- protein
- Length
- 83 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histone H1X
- UniProt
- Q92522
Structure
solution nmr · 1 distinct chain · 42% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histone H1X | protein | 83 | 42% helix, 12% strand | Q92522 |
Compared structures
- 2LSO · Solution NMR Structure of the Globular Domain of Human Histone H1x, Northeast Structural… · the same entry in another collection · chain A against A, TM-score 1.00
- Q92522 · AlphaFold monomer V2.0 prediction for histone H1.10 (Q92522) · a predicted model of the same protein · chain A against A, TM-score 0.81
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 Q92522
- Elsewhere: RCSB PDB 2LSO · PDBe 2LSO · UniProt Q92522
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