The crystal structure of the Human SNF5/INI1 domain. Determined by X-ray diffraction at 2.1 Å resolution. Released 10 May 2017.
Explore 5L7A in 3D Show helices and sheets RCSB PDB PDBe
5L7A contains 9 α-helices and 8 β-strands across 4 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 | 186-195 | 10 | 1 |
| β-strand | 198-207 | 10 | 1 |
| α-helix | 215-225 | 11 | |
| α-helix | 230-245 | 16 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 186-195 | 10 | 2 |
| β-strand | 198-207 | 10 | 2 |
| α-helix | 215-226 | 12 | |
| α-helix | 230-244 | 15 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 182-184 | 3 | |
| β-strand | 186-195 | 10 | 2 |
| β-strand | 198-207 | 10 | 2 |
| α-helix | 215-226 | 12 | |
| α-helix | 230-247 | 18 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 186-195 | 10 | 1 |
| β-strand | 198-207 | 10 | 1 |
| α-helix | 215-225 | 11 | |
| α-helix | 230-247 | 18 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1 | A, B, C, D | protein | 72 | Homo sapiens | Q12824 (AlphaFold model) |
>5L7A_1 SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1 (chains A, B, C, D) GGSEVLVPIRLDMEIDGQKLRDAFTWNMNEKLMTPEMFSEILCDDLDLNPLTFVPAIASA IRQQIESYPTDS
The structure of INI1/hSNF5 RPT1 and its interactions with the c-MYC:MAX heterodimer provide insights into the interplay between MYC and the SWI/SNF chromatin remodeling complex. Sammak, S., Allen, M.D., Hamdani, N. et al. FEBS J (2018) 285:4165-4180. DOI 10.1111/febs.14660 · PubMed
Other PDB entries of the same protein (UniProt Q12824 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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