› 3v56

X-ray diffraction
3Å resolution

Re-refinement of PDB entry 1OSG - Complex between BAFF and a BR3 derived peptide presented in a beta-hairpin scaffold - reveals an additonal copy of the peptide.

Released:
DOI: 10.2210/pdb3v56/pdb
PDB 3v56 coloured by chain and viewed from the front.
PDB 3v56 coloured by chain and viewed from the side.
PDB 3v56 coloured by chain and viewed from the top.
Source organism: Homo sapiens
Primary publication:
Exploiting structure similarity in refinement: automated NCS and target-structure restraints in BUSTER.
Smart OS, Womack TO, Flensburg C, Keller P, Paciorek W, Sharff A, Vonrhein C, Bricogne G
OpenAccess logo Acta Crystallogr. D Biol. Crystallogr. 68 368-80 (2012)
PMID: 22505257

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
Non-polymer only hexamer (preferred)
monomeric
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Tumor necrosis factor ligand superfamily member 13b, membrane form Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 208 amino acids
Theoretical weight: 22.75 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9Y275 (Residues: 82-285; Coverage: 72%)
Gene names: BAFF, BLYS, TALL1, TNFSF13B, TNFSF20, UNQ401/PRO738, ZTNF4
Sequence domains: TNF(Tumour Necrosis Factor) family
Structure domains: Jelly Rolls
Tumor necrosis factor receptor superfamily member 13C Chains: G, H, I, J, K, L, Z
Molecule details ›
Chains: G, H, I, J, K, L, Z
Length: 14 amino acids
Theoretical weight: 1.59 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q96RJ3 (Residues: 24-24, 25-35; Coverage: 6%)
Gene names: BAFFR, BR3, TNFRSF13C

Ligands and Environments

1 bound ligand:
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P65
Unit cell:
a: 121.633Å b: 121.633Å c: 157.214Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.165 0.162 0.2
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided

Quick links

Citations

2 review citations

The integrative role of cryo electron microscopy in molecular and cellular structural biology.
Orlov et al. (2017)
1 more

1 mention without citation

Exploiting structure similarity in refinement: automated NCS and target-structure restraints in BUSTER.
Smart et al. (2012)