Crystal structure of SGF29 tandem tudor domain in complex with a Carba containing peptide. Determined by X-ray diffraction at 1.6 Å resolution. Released 1 Jul 2015.
Explore 5C0M in 3D Show helices and sheets RCSB PDB PDBe
5C0M contains 29 α-helices and 32 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 | 115-129 | 15 | |
| α-helix | 131 | 1 | |
| β-strand | 132 | 1 | 1 |
| α-helix | 133 | 1 | |
| α-helix | 141-142 | 2 | |
| 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 |
| α-helix | 201-202 | 2 | |
| β-strand | 203-206 | 4 | 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 | |
| α-helix | 228-229 | 2 | |
| β-strand | 233-237 | 5 | 3 |
| α-helix | 238 | 1 | |
| β-strand | 243-251 | 9 | 3 |
| α-helix | 258-259 | 2 | |
| 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 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 117-129 | 13 | |
| α-helix | 131 | 1 | |
| β-strand | 132 | 1 | 5 |
| α-helix | 133 | 1 | |
| α-helix | 141-142 | 2 | |
| β-strand | 145 | 1 | 6 |
| α-helix | 148-151 | 4 | |
| α-helix | 156-157 | 2 | |
| β-strand | 161-167 | 7 | 7 |
| α-helix | 168 | 1 | |
| β-strand | 173-184 | 12 | 7 |
| β-strand | 189-194 | 6 | 7 |
| β-strand | 202-206 | 5 | 7 |
| α-helix | 207-209 | 3 | |
| β-strand | 210-212 | 3 | 7 |
| α-helix | 213-214 | 2 | |
| β-strand | 216 | 1 | 6 |
| β-strand | 217 | 1 | 5 |
| α-helix | 224-226 | 3 | |
| β-strand | 233-237 | 5 | 7 |
| α-helix | 238 | 1 | |
| β-strand | 243-251 | 9 | 7 |
| α-helix | 258-259 | 2 | |
| β-strand | 260-264 | 5 | 7 |
| β-strand | 265 | 1 | 8 |
| β-strand | 273 | 1 | 8 |
| α-helix | 274-276 | 3 | |
| β-strand | 277-279 | 3 | 7 |
| α-helix | 281-283 | 3 | |
| β-strand | 284-286 | 3 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| SAGA-associated factor 29 homolog | A, B | protein | 180 | Homo sapiens | Q96ES7 (AlphaFold model) |
| Carba-containing peptide | C, D | protein | 10 | Homo sapiens |
>5C0M_1 SAGA-associated factor 29 homolog (chains A, B) GRRGVLMTLLQQSAMTLPLWIGKPGDKPPPLCGAIPASGDYVARPGDKVAARVKAVDGDE QWILAEVVSYSHATNKYEVDDIDEEGKERHTLSRRRVIPLPQWKANPETDPEALFQKEQL VLALYPQTTCFYRALIHAPPQRPQDDYSVLFEDTSYADGYSPPLNVAQRYVVACKEPKKK
>5C0M_2 Carba-containing peptide (chains C, D) ARTXQTARKS
Chemical basis for the recognition of trimethyllysine by epigenetic reader proteins. Kamps, J.J., Huang, J., Poater, J. et al. Nat Commun (2015) 6:8911-8911. DOI 10.1038/ncomms9911 · 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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