› 6usb

X-ray diffraction
1.68Å resolution

Barrier-to-autointegration factor soaked in urea: 1 of 14 in MSCS set

Released:
DOI: 10.2210/pdb6usb/pdb
PDB entry 6usb coloured by chain, front view.
PDB entry 6usb coloured by chain, side view.
PDB entry 6usb coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Development of a structure-analysis pipeline using multiple-solvent crystal structures of barrier-to-autointegration factor.
Agarwal S, Smith M, De La Rosa I, Verba KA, Swartz P, Segura-Totten M, Mattos C
Acta Crystallogr D Struct Biol 76 1001-1014 (2020)
PMID: 33021502

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-131036 (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: 10.07 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O75531 (Residues: 1-89; Coverage: 100%)
Gene names: BAF, BANF1, BCRG1
Sequence domains: Barrier to autointegration factor

Ligands and Environments

1 bound ligand:
Ligand EOH 2 x EOH
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P43212
Unit cell:
a: 41.85Å b: 41.85Å c: 214.41Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.168 0.164 0.21
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Pharmacological Chaperones and Protein Conformational Diseases: Approaches of Computational Structural Biology.
Grasso et al. (2023)