Research workbench
Homo-and heteronuclear two-dimensional NMR studies of the globular domain of histone H1: full assignment, tertiary structure, and comparison with the globular domain of histone H5
Analyse Homo-and heteronuclear two-dimensional NMR studies of the globular domain of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1GHC
- Type
- protein
- Length
- 75 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P08287
Structure
solution nmr · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 75 | — | P08287 |
Compared structures
- 1GHC · Homo-and heteronuclear two-dimensional NMR studies of the globular domain of histone H1… · the same entry in another collection · chain A against A, TM-score 1.00
- P08287 · AlphaFold monomer V2.0 prediction for histone H1.11L (P08287) · a predicted model of the same protein · chain A against A, TM-score 0.63
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 P08287
- Elsewhere: RCSB PDB 1GHC · PDBe 1GHC · UniProt P08287
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