Loop deletion mutant (deleting four residues). Determined by X-ray diffraction at 1.4 Å resolution. Released 3 Jul 2019.
Explore 6ICS in 3D Show helices and sheets RCSB PDB PDBe
6ICS contains 2 α-helices and 23 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 | 29-34 | 6 | 1 |
| β-strand | 38-43 | 6 | 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 | 97-102 | 6 | 1 |
| β-strand | 109-115 | 7 | 1 |
| β-strand | 121-126 | 6 | 1 |
| β-strand | 132-138 | 7 | 1 |
| β-strand | 144-148 | 5 | 1 |
| β-strand | 156-162 | 7 | 1 |
| β-strand | 165-171 | 7 | 1 |
| β-strand | 175-182 | 8 | 1 |
| β-strand | 185-192 | 8 | 1 |
| β-strand | 197-203 | 7 | 1 |
| β-strand | 208-213 | 6 | 2 |
| β-strand | 218-223 | 6 | 2 |
| β-strand | 226-233 | 8 | 2 |
| β-strand | 239-243 | 5 | 2 |
| β-strand | 244 | 1 | 3 |
| α-helix | 245 | 1 | |
| β-strand | 251 | 1 | 3 |
| β-strand | 256-257 | 2 | 2 |
| α-helix | 261-267 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Outer surface protein A | O | protein | 247 | Borrelia burgdorferi | P0CL66 (AlphaFold model) |
>6ICS_1 Outer surface protein A (chains O) GSHMKNSVSVDLPGSMKVLVSKSSNADGKYDLIATVDALELSGTSDKNNGSGVLEGVKAD ASKVKLTISDDLGQTTLEVFKSDGSTLVSKKVTSKDKSSTEEKFNEKGEVSEKIITRADG TRLEYTGIKSDGSGKAKEVLKGYVLEGTLTAEKTTLVVKEGTVTLSKNISKSGAVSVELN DTDTKKTAAWNSGTSTLTITVNSKKTKDLVFTSSNTITVQQYDSNGTSLEGSAVEITKLD EIKNALK
Domain-Swapping Design by Polyproline Rod Insertion. Shiga, S., Yamanaka, M., Fujiwara, W. et al. Chembiochem (2019) 20:2454-2457. DOI 10.1002/cbic.201900179 · 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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