Crystal structure of the SGF29 in complex with H3K4me3. Determined by X-ray diffraction at 1.26 Å resolution. Released 28 Apr 2010.
Explore 3MEA in 3D Show helices and sheets RCSB PDB PDBe
3MEA contains 12 α-helices and 16 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 | 129-131 | 3 | |
| β-strand | 132 | 1 | 1 |
| α-helix | 133 | 1 | |
| α-helix | 135-136 | 2 | |
| α-helix | 139-142 | 4 | |
| β-strand | 145 | 1 | 2 |
| α-helix | 148-151 | 4 | |
| α-helix | 156-157 | 2 | |
| β-strand | 161-167 | 7 | 3 |
| β-strand | 173-184 | 12 | 3 |
| β-strand | 189-194 | 6 | 3 |
| β-strand | 201-206 | 6 | 3 |
| α-helix | 207-209 | 3 | |
| β-strand | 210-212 | 3 | 3 |
| α-helix | 213-214 | 2 | |
| β-strand | 216 | 1 | 2 |
| β-strand | 217 | 1 | 1 |
| α-helix | 224-226 | 3 | |
| β-strand | 233-237 | 5 | 3 |
| α-helix | 238 | 1 | |
| β-strand | 243-251 | 9 | 3 |
| β-strand | 260-264 | 5 | 3 |
| β-strand | 265 | 1 | 4 |
| β-strand | 273 | 1 | 4 |
| α-helix | 274-276 | 3 | |
| β-strand | 277-279 | 3 | 3 |
| α-helix | 281-283 | 3 | |
| β-strand | 284-286 | 3 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| SAGA-associated factor 29 homolog | A | protein | 180 | Homo sapiens | Q96ES7 (AlphaFold model) |
| Histone H3 | B | protein | 11 | Xenopus laevis | Q92133 (AlphaFold model) |
>3MEA_1 SAGA-associated factor 29 homolog (chains A) MHHHHHHSSRENLYFQGTLPLWIGKPGDKPPPLCGAIPASGDYVARPGDKVAARVKAVDG DEQWILAEVVSYSHATNKYEVDDIDEEGKERHTLSRRRVIPLPQWKANPETDPEALFQKE QLVLALYPQTTCFYRALIHAPPQRPQDDYSVLFEDTSYADGYSPPLNVAQRYVVACKEPK
>3MEA_2 Histone H3 (chains B) ARTKQTARKST
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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