2fkj

X-ray diffraction
3.1Å resolution

The crystal structure of engineered OspA

Released:
Source organism: Borreliella burgdorferi
Primary publication:
Atomic structures of peptide self-assembly mimics.
Proc Natl Acad Sci U S A 103 17753-8 (2006)
PMID: 17093048

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo trimer (preferred)
PDBe Complex ID:
PDB-CPX-143542 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Outer surface protein A Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 366 amino acids
Theoretical weight: 40.22 KDa
Source organism: Borreliella burgdorferi
Expression system: Escherichia coli
UniProt:
  • Canonical: P0CL66 (Residues: 27-131, 132-273; Coverage: 96%)
Gene names: BB_A15, ospA
Sequence domains: Borrelia lipoprotein
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: P21
Unit cell:
a: 72.15Å b: 105.5Å c: 88.981Å
α: 90° β: 93.24° γ: 90°
R-values:
R R work R free
0.249 0.247 0.282
Expression system: Escherichia coli