› 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 entry 3v56 coloured by chain, front view.
PDB entry 3v56 coloured by chain, side view.
PDB entry 3v56 coloured by chain, top view.
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
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:
hetero hexamer (preferred)
monomeric
Assembly name:
PDBe Complex ID:
PDB-CPX-188726 (preferred)
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
Sequence domains: BAFF-R, TALL-1 binding

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

3 review citations

Advances, interactions, and future developments in the CNS, Phenix, and Rosetta structural biology software systems.
Adams et al. (2013)
2 more

3 mentions without citation

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