› 1ghc

Solution NMR

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

Released:
DOI: 10.2210/pdb1ghc/pdb
PDB entry 1ghc coloured by chain, ensemble of 14 models, front view.
PDB entry 1ghc coloured by chain, ensemble of 14 models, side view.
PDB entry 1ghc coloured by chain, ensemble of 14 models, top view.
Source organism: Gallus gallus
Primary publication:
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.
Cerf C, Lippens G, Ramakrishnan V, Muyldermans S, Segers A, Wyns L, Wodak SJ, Hallenga K
Biochemistry 33 11079-86 (1994)
PMID: 7727360

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140084 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histone H1.11L Chain: A
Molecule details ›
Chain: A
Length: 75 amino acids
Theoretical weight: 7.69 KDa
Source organism: Gallus gallus
Expression system: Not provided
UniProt:
  • Canonical: P08287 (Residues: 41-114; Coverage: 33%)
Sequence domains: linker histone H1 and H5 family
Structure domains: Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Expression system: Not provided

Quick links

Citations

15 review citations

Forkhead transcription factors: key players in development and metabolism.
Carlsson et al. (2002)
14 more

14 mentions without citation

Multifunctionality of the linker histones: an emerging role for protein-protein interactions.
McBryant et al. (2010)
13 more