X-ray crystal structure of the human anti-apoptotic protein survivin. Determined by X-ray diffraction at 2.58 Å resolution. Released 6 Dec 2000.
Explore 1F3H in 3D Show helices and sheets RCSB PDB PDBe
1F3H contains 13 α-helices and 10 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 | 8-13 | 6 | |
| α-helix | 15-19 | 5 | |
| α-helix | 35-39 | 5 | |
| β-strand | 43-45 | 3 | 1 |
| β-strand | 48 | 1 | 2 |
| β-strand | 51 | 1 | 2 |
| β-strand | 55-57 | 3 | 1 |
| β-strand | 63-64 | 2 | 1 |
| α-helix | 73-80 | 8 | |
| α-helix | 86-88 | 3 | |
| α-helix | 93-95 | 3 | |
| β-strand | 97 | 1 | 3 |
| α-helix | 98-136 | 39 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 11-13 | 3 | |
| α-helix | 15-20 | 6 | |
| β-strand | 43-45 | 3 | 4 |
| β-strand | 55-57 | 3 | 4 |
| β-strand | 63-64 | 2 | 4 |
| α-helix | 73-78 | 6 | |
| α-helix | 85-88 | 4 | |
| α-helix | 93-95 | 3 | |
| β-strand | 97 | 1 | 3 |
| α-helix | 98-136 | 39 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Survivin | A, B | protein | 142 | Homo sapiens | O15392 (AlphaFold model) |
>1F3H_1 SURVIVIN (chains A, B) MGAPTLPPAWQPFLKDHRISTFKNWPFLEGCACTPERMAEAGFIHCPTENEPDMAQCFFC FKELEGWEPDDDPIEEHKKHSSGCAFLSVKKQFEELTLGEFLKLDRERAKNKIAKETNNK KKEFEETAKKVRRAIEQLAAMD
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 2 |
Water and common crystallization additives (SO4) are not listed.
Structure of the human anti-apoptotic protein survivin reveals a dimeric arrangement. Verdecia, M.A., Huang, H., Dutil, E. et al. Nat Struct Biol (2000) 7:602-608. DOI 10.1038/77929 · 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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