The complement inhibitory domain of B. burgdorferi BBK32. Determined by X-ray diffraction at 1.72 Å resolution. Released 27 Mar 2019.
Explore 6N1L in 3D Show helices and sheets RCSB PDB PDBe
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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| 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 |
| 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) |
>6N1L_1 Fibronectin-binding protein BBK32 (chains A) GSTGSSNRYQSYLEGVKYNVDSAIQTITKIYNTYTLFSTKLTQMYSTRLDNFAKAKAKEE AAKFTKEDLEKNFKTLLNYIQVSVKTAANFVYINDTHAKRKLENIEAEIKTLIAKIKEQS NLYEAYKAIVTSILLMRDSLKEVQGIID
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:
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