Circular Permuted Streptavidin A50/N49. Determined by X-ray diffraction at 1.0 Å resolution. Released 5 Jun 2013.
Explore 4GDA in 3D Show helices and sheets RCSB PDB PDBe
4GDA contains 5 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 | 54-60 | 7 | 1 |
| 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 | 123-132 | 10 | 1 |
| α-helix | 213-217 | 5 | |
| β-strand | 219-223 | 5 | 1 |
| β-strand | 228-233 | 6 | 1 |
| β-strand | 238-244 | 7 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 53-60 | 8 | 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 |
| β-strand | 219-223 | 5 | 2 |
| β-strand | 228-233 | 6 | 2 |
| β-strand | 238-244 | 7 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Streptavidin | A, B | protein | 131 | Streptomyces avidinii | P22629 (AlphaFold model) |
>4GDA_1 Streptavidin (chains A, B) AESRYVLTGRYDSAPATDGSGTALGWTVAWKNNYRNAHSATTWSGQYVGGAEARINTQWL LTSGTTEANAWKSTLVGHDTFTKVKPSAASGGGSAEAGITGTWYNQLGSTFIVTAGADGA LTGTYESAVGN
Water and common crystallization additives (SO4, GOL) are not listed.
Structural consequences of cutting a binding loop: two circularly permuted variants of streptavidin. Le Trong, I., Chu, V., Xing, Y. et al. Acta Crystallogr D Biol Crystallogr (2013) 69:968-977. DOI 10.1107/S0907444913003855 · 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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