3asw

X-ray diffraction
2.6Å resolution

Structural and biochemical characterization of ClfB:ligand interactions

Released:
Entry author: Ganesh VK

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Clumping factor B Chain: A
Molecule details ›
Chain: A
Length: 328 amino acids
Theoretical weight: 36.67 KDa
Source organism: Staphylococcus aureus subsp. aureus N315
Expression system: Escherichia coli
UniProt:
  • Canonical: Q7A382 (Residues: 212-531; Coverage: 38%)
Gene names: SA2423, clfB
Sequence domains:
Structure domains:
Keratin, type I cytoskeletal 10 Chain: B
Molecule details ›
Chain: B
Length: 15 amino acids
Theoretical weight: 1.18 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P13645 (Residues: 473-487; Coverage: 3%)
Gene names: KPP, KRT10

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P43
Unit cell:
a: 85.598Å b: 85.598Å c: 84.795Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.184 0.182 0.219
Expression systems:
  • Escherichia coli
  • Not provided