The structure of the F64A, S172A mutant Keap1-BTB domain in complex with SKP1-FBXL17. Determined by X-ray diffraction at 3.21 Å resolution. Released 19 Aug 2020.
Explore 6W66 in 3D Show helices and sheets RCSB PDB PDBe
6W66 contains 37 α-helices and 21 β-strands across 3 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 | 4-7 | 4 | 1 |
| β-strand | 13-16 | 4 | 1 |
| α-helix | 18-21 | 4 | |
| α-helix | 25-34 | 10 | |
| α-helix | 43-44 | 2 | |
| β-strand | 45-46 | 2 | 1 |
| α-helix | 52-64 | 13 | |
| α-helix | 68-70 | 3 | |
| α-helix | 87-92 | 6 | |
| α-helix | 97-109 | 13 | |
| α-helix | 113-127 | 15 | |
| α-helix | 132-139 | 8 | |
| α-helix | 149-156 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 321-323 | 3 | |
| α-helix | 326-334 | 9 | |
| α-helix | 338-342 | 5 | |
| α-helix | 345-347 | 3 | |
| α-helix | 350-357 | 8 | |
| β-strand | 365-366 | 2 | 2 |
| α-helix | 370-372 | 3 | |
| α-helix | 376-384 | 9 | |
| β-strand | 390-392 | 3 | 2 |
| α-helix | 401-410 | 10 | |
| β-strand | 416-418 | 3 | 2 |
| α-helix | 427-436 | 10 | |
| β-strand | 442-444 | 3 | 2 |
| α-helix | 456-462 | 7 | |
| β-strand | 468-472 | 5 | 2 |
| α-helix | 479-487 | 9 | |
| β-strand | 494-498 | 5 | 2 |
| α-helix | 505-512 | 8 | |
| β-strand | 520-524 | 5 | 2 |
| α-helix | 530-533 | 4 | |
| α-helix | 534-538 | 5 | |
| β-strand | 544-546 | 3 | 2 |
| α-helix | 555-564 | 10 | |
| β-strand | 570-572 | 3 | 2 |
| α-helix | 581-590 | 10 | |
| β-strand | 596-598 | 3 | 2 |
| α-helix | 606-615 | 10 | |
| β-strand | 621-623 | 3 | 2 |
| α-helix | 632-641 | 10 | |
| β-strand | 647-649 | 3 | 2 |
| α-helix | 658-667 | 10 | |
| β-strand | 672-674 | 3 | 2 |
| α-helix | 676-688 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 51-55 | 5 | 3 |
| α-helix | 59-61 | 3 | |
| α-helix | 63-72 | 10 | |
| β-strand | 79-83 | 5 | 4 |
| β-strand | 91-95 | 5 | 4 |
| α-helix | 97-103 | 7 | |
| α-helix | 105-111 | 7 | |
| β-strand | 121-125 | 5 | 4 |
| α-helix | 130-142 | 13 | |
| β-strand | 144-148 | 5 | 3 |
| α-helix | 152-162 | 11 | |
| α-helix | 165-177 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| S-phase kinase-associated protein 1 | A | protein | 163 | Homo sapiens | P63208 (AlphaFold model) |
| F-box/LRR-repeat protein 17 | B | protein | 396 | Homo sapiens | Q9UF56 (AlphaFold model) |
| Kelch-like ECH-associated protein 1 | C | protein | 134 | Homo sapiens | Q14145 (AlphaFold model) |
>6W66_1 S-phase kinase-associated protein 1 (chains A) MPSIKLQSSDGEIFEVDVEIAKQSVTIKTMLEDLGMDDEGDDDPVPLPNVNAAILKKVIQ WCTHHKDDPPPPEDDENKEKRTDDIPVWDQEFLKVDQGTLFELILAANYLDIKGLLDVTC KTVANMIKGKTPEEIRKTFNIKNDFTEEEEAQVRKENQWCEEK
>6W66_2 F-box/LRR-repeat protein 17 (chains B) GEFMCHREPPPETPDINQLPPSILLKIFSNLSLDERCLSASLVCKYWRDLCLDFQFWKQL DLSSRQQVTDELLEKIASRSQNIIEINISDCRSMSDNGVCVLAFKCPGLLRYTAYRCKQL SDTSIIAVASHCPLLQKVHVGNQDKLTDEGLKQLGSKCRELKDIHFGQCYKISDEGMIVI AKGCLKLQRIYMQENKLVTDQSVKAFAEHCPELQYVGFMGCSVTSKGVIHLTKLRNLSSL DLRHITELDNETVMEIVKRCKNLSSLNLCLNWIINDRCVEVIAKEGQNLKELYLVSCKIT DYALIAIGRYSMTIETVDVGWCKEITDQGATLIAQSSKSLRYLGLMRCDKVNEVTVEQLV QQYPHITFSTVLQDCKRTLERAYQMGWTPNMSAASS
>6W66_3 Kelch-like ECH-associated protein 1 (chains C) GGNRTFSYTLEDHTKQAAGIMNELRLSQQLCDVTLQVKYQDAPAAQFMAHKVVLASSSPV FKAMFTNGLREQGMEVVSIEGIHPKVMERLIEFAYTASISMGEKCVLHVMNGAVMYQIDS VVRACADFLVQQLD
Structural basis for dimerization quality control. Mena, E.L., Jevtic, P., Greber, B.J. et al. Nature (2020) 586:452-456. DOI 10.1038/s41586-020-2636-7 · PubMed
Other PDB entries of the same protein (UniProt P63208 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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