Wild-type core streptavidin-biotin complex at atomic resolution. Determined by X-ray diffraction at 0.95 Å resolution. Released 24 Aug 2011.
Explore 3RY2 in 3D Show helices and sheets RCSB PDB PDBe
3RY2 contains 6 α-helices and 16 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 |
|---|---|---|---|
| β-strand | 19-23 | 5 | 1 |
| β-strand | 28-33 | 6 | 1 |
| β-strand | 38-44 | 7 | 1 |
| β-strand | 54-60 | 7 | 1 |
| α-helix | 69-70 | 2 | |
| β-strand | 71-80 | 10 | 1 |
| β-strand | 85-97 | 13 | 1 |
| β-strand | 103-112 | 10 | 1 |
| α-helix | 113 | 1 | |
| α-helix | 116-121 | 6 | |
| β-strand | 123-133 | 11 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 19-23 | 5 | 2 |
| β-strand | 28-33 | 6 | 2 |
| β-strand | 38-44 | 7 | 2 |
| β-strand | 54-60 | 7 | 2 |
| β-strand | 71-80 | 10 | 2 |
| β-strand | 85-97 | 13 | 2 |
| β-strand | 103-112 | 10 | 2 |
| α-helix | 113 | 1 | |
| α-helix | 116-121 | 6 | |
| β-strand | 123-131 | 9 | 2 |
| α-helix | 133-135 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Streptavidin | A, B | protein | 127 | Streptomyces avidinii | P22629 (AlphaFold model) |
>3RY2_1 Streptavidin (chains A, B) AEAGITGTWYNQLGSTFIVTAGADGALTGTYESAVGNAESRYVLTGRYDSAPATDGSGTA LGWTVAWKNNYRNAHSATTWSGQYVGGAEARINTQWLLTSGTTEANAWKSTLVGHDTFTK VKPSAAS
| ID | Name | Formula | Copies |
|---|---|---|---|
| BTN | Biotin | C10 H16 N2 O3 S | 2 |
Water and common crystallization additives (GOL) are not listed.
Streptavidin and its biotin complex at atomic resolution. Le Trong, I., Wang, Z., Hyre, D.E. et al. Acta Crystallogr D Biol Crystallogr (2011) 67:813-821. DOI 10.1107/S0907444911027806 · PubMed
Other PDB entries of the same protein (UniProt P22629 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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