6N1L: Fibronectin-binding protein BBK32

The complement inhibitory domain of B. burgdorferi BBK32. Determined by X-ray diffraction at 1.72 Å resolution. Released 27 Mar 2019.

Method: X-ray diffraction
Resolution: 1.72 Å
Organism: Borrelia burgdorferi (strain ATCC 35210 / B31 / CIP 102532 / DSM 4680)
Chains: 1
Atoms: 1,265
Mol. weight: 16.92 kDa
Released: 27 Mar 2019

Explore 6N1L in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6N1L contains 5 α-helices and 0 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 5 helices, 0 β-strands

Element	Residues	Length
α-helix	209-244	36
α-helix	251-261	11
α-helix	266-287	22
α-helix	293-317	25
α-helix	322-347	26

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Fibronectin-binding protein BBK32	A	protein	148	Borrelia burgdorferi (strain ATCC 35210 / B31 / CIP 102532 / DSM 4680)	O50835 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>6N1L_1 Fibronectin-binding protein BBK32 (chains A)
GSTGSSNRYQSYLEGVKYNVDSAIQTITKIYNTYTLFSTKLTQMYSTRLDNFAKAKAKEE
AAKFTKEDLEKNFKTLLNYIQVSVKTAANFVYINDTHAKRKLENIEAEIKTLIAKIKEQS
NLYEAYKAIVTSILLMRDSLKEVQGIID

Primary citation

Structural determination of the complement inhibitory domain of Borrelia burgdorferi BBK32 provides insight into classical pathway complement evasion by lyme disease spirochetes. Xie, J., Zhi, H., Garrigues, R.J. et al. PLoS Pathog (2019) 15:e1007659-e1007659. DOI 10.1371/journal.ppat.1007659 · PubMed

Other PDB entries of the same protein (UniProt O50835 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4PZ5 1.96 Å, Crystal structure of the second and third fibronectin F1 modules in complex with a…
7MZT 4.07 Å, Borrelia burgdorferi BBK32-C in complex with an autolytic fragment of human C1r at 4.1A

Browse structure collections

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