The crystal structure of OspA mutant. Determined by X-ray diffraction at 1.55 Å resolution. Released 4 Mar 2008.
Explore 2OY7 in 3D Show helices and sheets RCSB PDB PDBe
2OY7 contains 3 α-helices and 29 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 |
|---|---|---|---|
| β-strand | 29-33 | 5 | 1 |
| α-helix | 35-37 | 3 | |
| β-strand | 39-43 | 5 | 1 |
| β-strand | 52-58 | 7 | 1 |
| β-strand | 61-67 | 7 | 1 |
| β-strand | 74-79 | 6 | 1 |
| β-strand | 85-90 | 6 | 1 |
| β-strand | 96-102 | 7 | 1 |
| β-strand | 109-116 | 8 | 1 |
| β-strand | 121-126 | 6 | 1 |
| β-strand | 132-138 | 7 | 1 |
| β-strand | 144-149 | 6 | 1 |
| β-strand | 155-161 | 7 | 1 |
| β-strand | 167-172 | 6 | 1 |
| β-strand | 178-184 | 7 | 1 |
| β-strand | 190-195 | 6 | 1 |
| β-strand | 201-207 | 7 | 1 |
| β-strand | 213-217 | 5 | 1 |
| β-strand | 225-231 | 7 | 1 |
| β-strand | 234-240 | 7 | 1 |
| β-strand | 244-251 | 8 | 1 |
| β-strand | 254-261 | 8 | 1 |
| β-strand | 266-272 | 7 | 1 |
| β-strand | 281-286 | 6 | 2 |
| β-strand | 291-296 | 6 | 2 |
| β-strand | 299-306 | 8 | 2 |
| β-strand | 312-316 | 5 | 2 |
| β-strand | 317 | 1 | 3 |
| α-helix | 318 | 1 | |
| β-strand | 324 | 1 | 3 |
| β-strand | 329-330 | 2 | 2 |
| α-helix | 334-341 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Outer surface protein A | A | protein | 320 | Borrelia burgdorferi | P0CL66 (AlphaFold model) |
>2OY7_1 Outer surface protein A (chains A) GSHMKNSVSVDLPGSMKVLVSKSSNADGKYDLIATVDALELSGTSDKNNGSGVLEGVKAD ASKVKLTISDDLGQTTLEVFKSDGSTLVSKKVTSKDKSSTYEKFNEKGELSEKYITRADK SSTYEKFNEKGELSEKYITRADKSSTYEKFNEKGELSEKYITRADKSSTYEKFNEKGEVS EKYITRADGTRLEYTGIKSDGSGKAKEVLKGYVLEGTLTAEKTTLVVKEGTVTLSKNISK SGEVSVELNDTDSSAATKKTAAWNSGTSTLTITVNSKKTKDLVFTSSNTITVQQYDSNGT SLEGSAVEITKLDEIKNALK
Aromatic cross-strand ladders control the structure and stability of beta-rich peptide self-assembly mimics. Biancalana, M., Makabe, K., Koide, A. et al. J Mol Biol (2008) 383:205-213. DOI 10.1016/j.jmb.2008.08.031 · PubMed
Other PDB entries of the same protein (UniProt P0CL66 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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