The structure of Sir2Af2 bound to a myristoylated histone peptide. Determined by X-ray diffraction at 1.65 Å resolution. Released 3 Dec 2014.
Explore 4TWJ in 3D Show helices and sheets RCSB PDB PDBe
4TWJ contains 15 α-helices and 17 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 | 2-14 | 13 | |
| β-strand | 18-22 | 5 | 1 |
| α-helix | 24-26 | 3 | |
| β-strand | 28 | 1 | 2 |
| α-helix | 48-51 | 4 | |
| β-strand | 52 | 1 | 3 |
| α-helix | 53-58 | 6 | |
| α-helix | 60-73 | 14 | |
| β-strand | 74 | 1 | 2 |
| α-helix | 80-90 | 11 | |
| β-strand | 94-99 | 6 | 1 |
| α-helix | 105-108 | 4 | |
| β-strand | 114-116 | 3 | 1 |
| β-strand | 119-126 | 8 | 4 |
| β-strand | 132-134 | 3 | 4 |
| α-helix | 135-137 | 3 | |
| α-helix | 139-143 | 5 | |
| α-helix | 146-148 | 3 | |
| β-strand | 158-162 | 5 | 4 |
| β-strand | 165 | 1 | 3 |
| β-strand | 168 | 1 | 5 |
| α-helix | 169-170 | 2 | |
| α-helix | 171-182 | 12 | |
| β-strand | 186-190 | 5 | 1 |
| β-strand | 196-197 | 2 | 6 |
| α-helix | 201-208 | 8 | |
| β-strand | 212-217 | 6 | 1 |
| α-helix | 224-226 | 3 | |
| β-strand | 229-232 | 4 | 1 |
| α-helix | 235-249 | 15 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4 | 1 | 5 |
| β-strand | 6-7 | 2 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| NAD-dependent protein deacylase 2 | A | protein | 253 | Archaeoglobus fulgidus | O30124 (AlphaFold model) |
| Histone H4 peptide | B | protein | 14 | Saccharomyces cerevisiae | P02309 (AlphaFold model) |
>4TWJ_1 NAD-dependent protein deacylase 2 (chains A) MEDEIRKAAEILAKSKHAVVFTGAGISAESGIPTFRGEDGLWRKYDPEEVASISGFKRNP RAFWEFSMEMKDKLFAEPNPAHYAIAELERMGIVKAVITQNIDMLHQRAGSRRVLELHGS MDKLDCLDCHETYDWSEFVEDFNKGEIPRCRKCGSYYVKPRVVLFGEPLPQRTLFEAIEE AKHCDAFMVVGSSLVVYPAAELPYIAKKAGAKMIIVNAEPTMADPIFDVKIIGKAGEVLP KIVEEVKRLRSEK
>4TWJ_2 Histone H4 peptide (chains B) KGLGKGGAXRHRKW
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 1 |
Water and common crystallization additives (GOL, ACT) are not listed.
Alternate deacylating specificities of the archaeal sirtuins Sir2Af1 and Sir2Af2. Ringel, A.E., Roman, C., Wolberger, C. Protein Sci (2014) 23:1686-1697. DOI 10.1002/pro.2546 · PubMed
Other PDB entries of the same protein (UniProt O30124 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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