Cryatal structure of OspC3 C-terminal ankyrin-repeat domain. Determined by X-ray diffraction at 1.54 Å resolution. Released 25 Jan 2023.
Explore 7WR2 in 3D Show helices and sheets RCSB PDB PDBe
7WR2 contains 13 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 | 348-353 | 6 | |
| α-helix | 357-363 | 7 | |
| α-helix | 367-379 | 13 | |
| α-helix | 383-392 | 10 | |
| α-helix | 397-403 | 7 | |
| α-helix | 410-414 | 5 | |
| α-helix | 417-422 | 6 | |
| α-helix | 425-427 | 3 | |
| α-helix | 428-436 | 9 | |
| α-helix | 444-446 | 3 | |
| α-helix | 455-462 | 8 | |
| α-helix | 465-473 | 9 | |
| α-helix | 478-480 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| OspC3 | A | protein | 161 | Shigella flexneri | A0A0H2US87 (AlphaFold model) |
>7WR2_1 OspC3 (chains A) GPLGSGRPMLSTDNFKKIKLRDISLEDAIKASNYEEINNKVTDKKMAHQALAYSLGNKKA DIALYLLSKFNFTKQDVAEMEKMKNNRYCNLYDVEYLLSKDGANYKVLEYFINNGLVDVN KKFQKVNSGDTMLDNAMKSKDSKMIDFLLKNGAILGKRFEI
Structural mechanisms of calmodulin activation of Shigella effector OspC3 to ADP-riboxanate caspase-4/11 and block pyroptosis. Hou, Y., Zeng, H., Li, Z. et al. Nat Struct Mol Biol (2023) 30:261-272. DOI 10.1038/s41594-022-00888-3 · PubMed
Other PDB entries of the same protein (UniProt A0A0H2US87 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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