› 6fy5

X-ray diffraction
1.65Å resolution

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-192803 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Core histone macro-H2A.2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 198 amino acids
Theoretical weight: 21.3 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q9P0M6 (Residues: 178-372; Coverage: 52%)
Gene names: H2AFY2, MACROH2A2
Sequence domains: Macro domain
Structure domains: Leucine Aminopeptidase, subunit E, domain 1

Ligands and Environments

2 bound ligands:
Ligand ACT 2 x ACT
Ligand EDO 3 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P21
Unit cell:
a: 57.75Å b: 41.37Å c: 84.15Å
α: 90° β: 97.05° γ: 90°
R-values:
R R work R free
0.216 0.215 0.244
Expression system: Escherichia coli BL21

Quick links

Citations

18 review citations

The roles of histone variants in fine-tuning chromatin organization and function.
Martire et al. (2020)
17 more

2 mentions without citation

MacroH2A histone variants limit chromatin plasticity through two distinct mechanisms.
Kozlowski et al. (2018)
1 more