X-ray diffraction
2.92Å resolution

Crystal structure of the macro-domain of human core histone variant macroH2A1.2

Source organism: Homo sapiens
Primary publication:
Splicing regulates NAD metabolite binding to histone macroH2A.
Nat. Struct. Mol. Biol. 12 624-5 (2005)
PMID: 15965484

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Core histone macro-H2A.1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 214 amino acids
Theoretical weight: 22.71 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
  • Canonical: O75367 (Residues: 161-372; Coverage: 57%)
Gene names: H2AFY, MACROH2A1
Sequence domains: Macro domain
Structure domains: Leucine Aminopeptidase, subunit E, domain 1

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P212121
Unit cell:
a: 40.549Å b: 72.258Å c: 144.641Å
α: 90° β: 90° γ: 90°
R R work R free
0.216 0.213 0.277
Expression system: Escherichia coli BL21(DE3)