Crystal structure of human Survivin bound to histone H3 phosphorylated on threonine-3. Determined by X-ray diffraction at 2.18 Å resolution. Released 7 Mar 2012.
Explore 3UEC in 3D Show helices and sheets RCSB PDB PDBe
3UEC contains 7 α-helices and 4 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 | 11-13 | 3 | |
| α-helix | 15-20 | 6 | |
| α-helix | 35-40 | 6 | |
| β-strand | 43-45 | 3 | 1 |
| β-strand | 55-57 | 3 | 1 |
| β-strand | 63-65 | 3 | 1 |
| α-helix | 73-80 | 8 | |
| α-helix | 85-88 | 4 | |
| α-helix | 93-95 | 3 | |
| α-helix | 98-139 | 42 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-3 | 2 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Baculoviral IAP repeat-containing protein 5 | A | protein | 146 | Homo sapiens | O15392 (AlphaFold model) |
| N-terminal fragment of histone H3 | B | protein | 4 |
>3UEC_1 Baculoviral IAP repeat-containing protein 5 (chains A) GSHEMGAPTLPPAWQPFLKDHRISTFKNWPFLEGCACTPERMAEAGFIHCPTENEPDLAQ CFFCFKELEGWEPDDDPIEEHKKHSSGCAFLSVKKQFEELTLGEFLKLDRERAKNKIAKE TNNKKKEFEETAKKVRRAIEQLAAMD
>3UEC_2 N-TERMINAL FRAGMENT OF HISTONE H3 (chains B) ARTK
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 1 |
Water and common crystallization additives (PEG, ACT, 1PE, PG4, EDO) are not listed.
Molecular basis for phosphospecific recognition of histone H3 tails by Survivin paralogues at inner centromeres. Niedzialkowska, E., Wang, F., Porebski, P.J. et al. Mol Biol Cell (2012) 23:1457-1466. DOI 10.1091/mbc.E11-11-0904 · PubMed
Other PDB entries of the same protein (UniProt O15392 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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