2fxk

X-ray diffraction
2.54Å resolution

Crystal structure of the macro-domain of human core histone variant macroH2A1.1 (form A)

Released:
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 analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-130917 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Core histone macro-H2A.1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 211 amino acids
Theoretical weight: 22.27 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O75367 (Residues: 162-369; Coverage: 56%)
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: P21212
Unit cell:
a: 90.77Å b: 98.27Å c: 42.05Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.21 0.207 0.27
Expression system: Escherichia coli BL21(DE3)