› 3ckg

X-ray diffraction
1.8Å resolution

The crystal structure of OspA deletion mutant

Released:
DOI: 10.2210/pdb3ckg/pdb
PDB entry 3ckg coloured by chain, front view.
PDB entry 3ckg coloured by chain, side view.
PDB entry 3ckg coloured by chain, top view.
Source organism: Borreliella burgdorferi
Primary publication:
The promiscuity of beta-strand pairing allows for rational design of beta-sheet face inversion.
Makabe K, Koide S
J Am Chem Soc 130 14370-1 (2008)
PMID: 18842042

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-175039 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Outer surface protein A Chain: A
Molecule details ›
Chain: A
Length: 236 amino acids
Theoretical weight: 24.64 KDa
Source organism: Borreliella burgdorferi
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q45040 (Residues: 27-273; Coverage: 85%)
Gene name: ospA
Sequence domains: Borrelia lipoprotein
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand MG 1 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P21212
Unit cell:
a: 60.813Å b: 117.176Å c: 36.761Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.191 0.189 0.226
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

Engineering of recombinant crystallization chaperones.
Koide S. (2009)
1 more

1 mention without citation

Protein folding, misfolding and aggregation: The importance of two-electron stabilizing interactions.
Cieplak AS. (2017)