Coevolved affibody-Z domain pair LL2.c1. Determined by X-ray diffraction at 1.29 Å resolution. Released 26 Jul 2023.
Explore 8DA8 in 3D Show helices and sheets RCSB PDB PDBe
8DA8 contains 8 α-helices and 0 β-strands across 2 chains. 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 | 6-18 | 13 | |
| α-helix | 24-36 | 13 | |
| α-helix | 38-40 | 3 | |
| α-helix | 41-54 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 5-17 | 13 | |
| α-helix | 24-36 | 13 | |
| α-helix | 38-40 | 3 | |
| α-helix | 41-54 | 14 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Immunoglobulin G-binding protein A | A | protein | 67 | Staphylococcus aureus | P02976 (AlphaFold model) |
| Affibody LL2.FIIK | B | protein | 67 | synthetic construct |
>8DA8_1 Immunoglobulin G-binding protein A (chains A) AVDNKFNKELQNAVYEILHLPNLNEEQRNAFFQSLKDDPSQSANLLAEAKKLNDAQAPKL EHHHHHH
>8DA8_2 Affibody LL2.FIIK (chains B) AVDNKFNKEFSVAGREIITLPNLNDPQKKAFIKSLWDDPSQSANLLAEAKKLNDAQAPKL EHHHHHH
Deploying synthetic coevolution and machine learning to engineer protein-protein interactions. Yang, A., Jude, K.M., Lai, B. et al. Science (2023) 381:eadh1720-eadh1720. DOI 10.1126/science.adh1720 · PubMed
Other PDB entries of the same protein (UniProt P02976 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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