Crystal structure of a Novel Tudor domain-containing protein SGF29. Determined by X-ray diffraction at 1.78 Å resolution. Released 5 May 2010.
Explore 3LX7 in 3D Show helices and sheets RCSB PDB PDBe
3LX7 contains 11 α-helices and 14 β-strands across 1 chain. 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 | 141-142 | 2 | |
| β-strand | 145 | 1 | 1 |
| α-helix | 149-151 | 3 | |
| α-helix | 156-157 | 2 | |
| β-strand | 161-165 | 5 | 2 |
| β-strand | 175-184 | 10 | 2 |
| β-strand | 189-194 | 6 | 2 |
| β-strand | 202-206 | 5 | 2 |
| α-helix | 207-209 | 3 | |
| β-strand | 210-212 | 3 | 2 |
| α-helix | 213-214 | 2 | |
| β-strand | 216 | 1 | 1 |
| α-helix | 224-226 | 3 | |
| α-helix | 228-229 | 2 | |
| β-strand | 233-237 | 5 | 2 |
| α-helix | 238 | 1 | |
| β-strand | 243-251 | 9 | 2 |
| α-helix | 258-259 | 2 | |
| β-strand | 260-264 | 5 | 2 |
| β-strand | 265 | 1 | 3 |
| β-strand | 273 | 1 | 3 |
| α-helix | 274-276 | 3 | |
| β-strand | 277-279 | 3 | 2 |
| α-helix | 281-283 | 3 | |
| β-strand | 284-286 | 3 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| SAGA-associated factor 29 homolog | A | protein | 174 | Homo sapiens | Q96ES7 (AlphaFold model) |
>3LX7_1 SAGA-associated factor 29 homolog (chains A) MHHHHHHSSGRENLYFQGGDKPPPLCGAIPASGDYVARPGDKVAARVKAVDGDEQWILAE VVSYSHATNKYEVDDIDEEGKERHTLSRRRVIPLPQWKANPETDPEALFQKEQLVLALYP QTTCFYRALIHAPPQRPQDDYSVLFEDTSYADGYSPPLNVAQRYVVACKEPKKK
Sgf29 binds histone H3K4me2/3 and is required for SAGA complex recruitment and histone H3 acetylation. Bian, C., Xu, C., Ruan, J. et al. EMBO J (2011) 30:2829-2842. DOI 10.1038/emboj.2011.193 · PubMed
Other PDB entries of the same protein (UniProt Q96ES7 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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