5chl

X-ray diffraction
1.89Å resolution

Structural basis of H2A.Z recognition by YL1 histone chaperone component of SRCAP/SWR1 chromatin remodeling complex

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-142909 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Vacuolar protein sorting-associated protein 72 homolog Chain: A
Molecule details ›
Chain: A
Length: 74 amino acids
Theoretical weight: 8.59 KDa
Source organism: Drosophila melanogaster
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9VKM6 (Residues: 2-75; Coverage: 21%)
Gene names: CG4621, YL-1
Sequence domains: YL1 nuclear protein
Histone H2A.Z Chain: B
Molecule details ›
Chain: B
Length: 193 amino acids
Theoretical weight: 21.16 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P0C0S5 (Residues: 22-113; Coverage: 72%)
Gene names: H2AFZ, H2AZ, H2AZ1
Sequence domains:
Structure domains: Histone, subunit A

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: P41212
Unit cell:
a: 108.047Å b: 108.047Å c: 58.243Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.202 0.2 0.231
Expression system: Escherichia coli