Crystal Structure of the Tick Evasin EVA-AAM1001(Y44A) Complexed to Human Chemokine CCL7. Determined by X-ray diffraction at 1.74 Å resolution. Released 29 Mar 2023.
Explore 8FK6 in 3D Show helices and sheets RCSB PDB PDBe
8FK6 contains 6 α-helices and 15 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 |
|---|---|---|---|
| β-strand | 28-29 | 2 | 1 |
| β-strand | 31 | 1 | 2 |
| β-strand | 32-33 | 2 | 3 |
| β-strand | 40 | 1 | 2 |
| β-strand | 41-42 | 2 | 4 |
| β-strand | 45-48 | 4 | 5 |
| β-strand | 51-54 | 4 | 5 |
| α-helix | 55-56 | 2 | |
| β-strand | 60-63 | 4 | 4 |
| α-helix | 66-71 | 6 | |
| α-helix | 79 | 1 | |
| β-strand | 80-86 | 7 | 4 |
| β-strand | 89-97 | 9 | 4 |
| β-strand | 99-100 | 2 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 10-11 | 2 | 1 |
| α-helix | 22-24 | 3 | |
| β-strand | 25-31 | 7 | 6 |
| α-helix | 32-33 | 2 | |
| β-strand | 41-45 | 5 | 6 |
| β-strand | 50-53 | 4 | 6 |
| α-helix | 58-68 | 11 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Evasin P1243 | A | protein | 103 | Amblyomma americanum | A0A0C9S461 (AlphaFold model) |
| C-C motif chemokine 7 | B | protein | 76 | Homo sapiens | P80098 (AlphaFold model) |
>8FK6_1 Evasin P1243 (chains A) GSTSARNHTEDNSTEYYDYEEARCACPARHLNNTNGTVLKLLGCHAFCNGTLCTAPDGYP CYNLTAQQVRTLTTYPNTSCAVGVCMKGTCVKNGTMEQCFKTP
>8FK6_2 C-C motif chemokine 7 (chains B) QPVGINTSTTCCYRFINKKIPKQRLESYRRTTSSHCPREAVIFKTKLDKEICADPTQKWV QDFMKHLDKKTQTPKL
Engineering broad-spectrum inhibitors of inflammatory chemokines from subclass A3 tick evasins. Devkota, S.R., Aryal, P., Pokhrel, R. et al. Nat Commun (2023) 14:4204-4204. DOI 10.1038/s41467-023-39879-3 · PubMed
Other PDB entries of the same protein (UniProt A0A0C9S461 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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