2OY7: OspA mutant

The crystal structure of OspA mutant. Determined by X-ray diffraction at 1.55 Å resolution. Released 4 Mar 2008.

Method
X-ray diffraction
Resolution
1.55 Å
Organism
Borrelia burgdorferi
Chains
1
Atoms
2,832
Mol. weight
34.67 kDa
Released
4 Mar 2008

Explore 2OY7 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 3 helices, 29 β-strands

ElementResiduesLengthSheet
β-strand29-3351
α-helix35-373
β-strand39-4351
β-strand52-5871
β-strand61-6771
β-strand74-7961
β-strand85-9061
β-strand96-10271
β-strand109-11681
β-strand121-12661
β-strand132-13871
β-strand144-14961
β-strand155-16171
β-strand167-17261
β-strand178-18471
β-strand190-19561
β-strand201-20771
β-strand213-21751
β-strand225-23171
β-strand234-24071
β-strand244-25181
β-strand254-26181
β-strand266-27271
β-strand281-28662
β-strand291-29662
β-strand299-30682
β-strand312-31652
β-strand31713
α-helix3181
β-strand32413
β-strand329-33022
α-helix334-3418

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Outer surface protein AAprotein320Borrelia burgdorferiP0CL66 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2OY7_1 Outer surface protein A (chains A)
GSHMKNSVSVDLPGSMKVLVSKSSNADGKYDLIATVDALELSGTSDKNNGSGVLEGVKAD
ASKVKLTISDDLGQTTLEVFKSDGSTLVSKKVTSKDKSSTYEKFNEKGELSEKYITRADK
SSTYEKFNEKGELSEKYITRADKSSTYEKFNEKGELSEKYITRADKSSTYEKFNEKGEVS
EKYITRADGTRLEYTGIKSDGSGKAKEVLKGYVLEGTLTAEKTTLVVKEGTVTLSKNISK
SGEVSVELNDTDSSAATKKTAAWNSGTSTLTITVNSKKTKDLVFTSSNTITVQQYDSNGT
SLEGSAVEITKLDEIKNALK

Primary citation

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:

Browse structure collections

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