7cyu

X-ray diffraction
2.55Å resolution

Crystal structure of human BAF57 HMG domain

Released:
Source organism: Homo sapiens
Primary publication:
Crystal structure of the HMG domain of human BAF57 and its interaction with four-way junction DNA.
Biochem Biophys Res Commun 533 919-924 (2020)
PMID: 33010889

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-188331 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1 Chain: A
Molecule details ›
Chain: A
Length: 71 amino acids
Theoretical weight: 8.56 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q969G3 (Residues: 66-134; Coverage: 17%)
Gene names: BAF57, SMARCE1
Sequence domains: HMG (high mobility group) box

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 5C (4A)
Spacegroup: P3221
Unit cell:
a: 58.873Å b: 58.873Å c: 50.263Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.238 0.233 0.275
Expression system: Escherichia coli