1ci4

X-ray diffraction
1.9Å resolution

THE CRYSTAL STRUCTURE OF HUMAN BARRIER-TO-AUTOINTEGRATION FACTOR (BAF)

Released:
Source organism: Homo sapiens
Primary publication:
Structural basis of DNA bridging by barrier-to-autointegration factor.
Biochemistry 39 9130-8 (2000)
PMID: 10924106

Function and Biology Details

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Barrier-to-autointegration factor Chains: A, B
Molecule details ›
Chains: A, B
Length: 89 amino acids
Theoretical weight: 10.17 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O75531 (Residues: 1-89; Coverage: 100%)
Gene names: BAF, BANF1, BCRG1
Sequence domains: Barrier to autointegration factor
Structure domains: Barrier-to-autointegration factor, BAF

Ligands and Environments

No bound ligands
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X9B
Spacegroup: P43212
Unit cell:
a: 41.8Å b: 41.8Å c: 214.6Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.21 0.21 0.262
Expression system: Escherichia coli