› 1fj1

X-ray diffraction
2.68Å resolution

LYME DISEASE ANTIGEN OSPA IN COMPLEX WITH NEUTRALIZING ANTIBODY FAB LA-2

Released:
DOI: 10.2210/pdb1fj1/pdb
PDB entry 1fj1 coloured by chain, front view.
PDB entry 1fj1 coloured by chain, side view.
PDB entry 1fj1 coloured by chain, top view.
Source organisms:
Primary publication:
Structural identification of a key protective B-cell epitope in Lyme disease antigen OspA.
Ding W, Huang X, Yang X, Dunn JJ, Luft BJ, Koide S, Lawson CL
J Mol Biol 302 1153-64 (2000)
PMID: 11183781

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
PDBe Complex ID:
PDB-CPX-134670 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Immunoglobulin kappa constant Chains: A, C
Molecule details ›
Chains: A, C
Length: 213 amino acids
Theoretical weight: 23.61 KDa
Source organism: Mus musculus
UniProt:
  • Canonical: P01837 (Residues: 1-106; Coverage: 99%)
Gene name: Igkc
Sequence domains: Immunoglobulin C1-set domain
Structure domains: Immunoglobulins
Immunoglobulin heavy constant gamma 2B Chains: B, D
Molecule details ›
Chains: B, D
Length: 213 amino acids
Theoretical weight: 22.63 KDa
Source organism: Mus musculus
UniProt:
  • Canonical: P01867 (Residues: 1-99; Coverage: 25%)
Gene names: Igh-3, Ighg2b
Sequence domains: Immunoglobulin C1-set domain
Structure domains: Immunoglobulins
Outer surface protein A Chains: E, F
Molecule details ›
Chains: E, F
Length: 257 amino acids
Theoretical weight: 27.68 KDa
Source organism: Borreliella burgdorferi B31
Expression system: Escherichia coli
UniProt:
  • Canonical: P0CL66 (Residues: 18-273; Coverage: 100%)
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: NSLS BEAMLINE X25
Spacegroup: P21212
Unit cell:
a: 100.079Å b: 129.462Å c: 143.738Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.226 0.226 0.281
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Quantitative account of the enhanced affinity of two linked scFvs specific for different epitopes on the same antigen.
Zhou HX. (2003)
5 more

13 mentions without citation

An accurate, residue-level, pair potential of mean force for folding and binding based on the distance-scaled, ideal-gas reference state.
Zhang et al. (2004)
12 more