Higher resolution structure of the N-terminal module of the human SWI/SNF-subunit BAF155/SMARCC1. Determined by X-ray diffraction at 1.6 Å resolution. Released 21 Apr 2021.
Explore 6YXP in 3D Show helices and sheets RCSB PDB PDBe
6YXP contains 38 α-helices and 22 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 | 28-31 | 4 | |
| α-helix | 40-44 | 5 | |
| α-helix | 46-51 | 6 | |
| α-helix | 53-62 | 10 | |
| α-helix | 64-67 | 4 | |
| α-helix | 74-92 | 19 | |
| α-helix | 102-105 | 4 | |
| α-helix | 106-109 | 4 | |
| α-helix | 117-131 | 15 | |
| α-helix | 146-161 | 16 | |
| β-strand | 169-172 | 4 | 1 |
| α-helix | 178-190 | 13 | |
| β-strand | 194-195 | 2 | 1 |
| α-helix | 199-201 | 3 | |
| β-strand | 204-207 | 4 | 1 |
| β-strand | 218-225 | 8 | 2 |
| β-strand | 228-233 | 6 | 2 |
| α-helix | 238-240 | 3 | |
| β-strand | 242-245 | 4 | 2 |
| α-helix | 246-248 | 3 | |
| α-helix | 252-259 | 8 | |
| β-strand | 263-266 | 4 | 1 |
| α-helix | 268-276 | 9 | |
| α-helix | 279-281 | 3 | |
| α-helix | 282-285 | 4 | |
| β-strand | 286 | 1 | 1 |
| β-strand | 287 | 1 | 3 |
| β-strand | 293 | 1 | 3 |
| α-helix | 298-299 | 2 | |
| β-strand | 300-301 | 2 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 28-31 | 4 | |
| α-helix | 40-44 | 5 | |
| α-helix | 46-62 | 17 | |
| α-helix | 64-67 | 4 | |
| α-helix | 74-92 | 19 | |
| α-helix | 102-105 | 4 | |
| α-helix | 106-109 | 4 | |
| α-helix | 117-132 | 16 | |
| α-helix | 142-144 | 3 | |
| α-helix | 145-161 | 17 | |
| β-strand | 169-172 | 4 | 4 |
| α-helix | 178-190 | 13 | |
| β-strand | 194-195 | 2 | 4 |
| α-helix | 199-201 | 3 | |
| β-strand | 204-207 | 4 | 4 |
| β-strand | 218-225 | 8 | 5 |
| β-strand | 228-233 | 6 | 5 |
| α-helix | 238-240 | 3 | |
| β-strand | 242-245 | 4 | 5 |
| α-helix | 251-257 | 7 | |
| α-helix | 260 | 1 | |
| β-strand | 263-266 | 4 | 4 |
| α-helix | 268-276 | 9 | |
| α-helix | 279-281 | 3 | |
| α-helix | 282-285 | 4 | |
| β-strand | 286 | 1 | 4 |
| β-strand | 287 | 1 | 6 |
| β-strand | 293 | 1 | 6 |
| α-helix | 298-299 | 2 | |
| β-strand | 300-301 | 2 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| SWI/SNF complex subunit SMARCC1 | A, B | protein | 280 | Homo sapiens | Q92922 (AlphaFold model) |
>6YXP_1 SWI/SNF complex subunit SMARCC1 (chains A, B) GSLAVYRRKDGGPATKFWESPETVSQLDSVRVWLGKHYKKYVHADAPTNKTLAGLVVQLL QFQEDAFGKHVTNPAFTKLPAKCFMDFKAGGALCHILGAAYKYKNEQGWRRFDLQNPSRM DRNVEMFMNIEKTLVQNNCLTRPNIYLIPDIDLKLANKLKDIIKRHQGTFTDEKSKASHH IYPYSSSQDDEEWLRPVMRKEKQVLVHWGFYPDSYDTWVHSNDVDAEIEDPPIPEKPWKV HVKWILDTDIFNEWMNEEDYEVDENRKPVSFRQRISTKNE
SWI/SNF subunit BAF155 N-terminus structure informs the impact of cancer-associated mutations and reveals a potential drug binding site. Allen, M.D., Freund, S.M.V., Bycroft, M. et al. Commun Biol (2021) 4:528-528. DOI 10.1038/s42003-021-02050-z · PubMed
Other PDB entries of the same protein (UniProt Q92922 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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