Structural origins of high-affinity biotin binding to streptavidin. Determined by X-ray diffraction at 2.6 Å resolution. Released 15 Oct 1992.
Explore 1STP in 3D Show helices and sheets RCSB PDB PDBe
1STP contains 3 α-helices and 8 β-strands across 1 chain. 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 | 14-17 | 4 | |
| 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 | 116-121 | 6 | |
| β-strand | 123-131 | 9 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Streptavidin complex with biotin | A | protein | 159 | Streptomyces avidinii | P22629 (AlphaFold model) |
>1STP_1 STREPTAVIDIN COMPLEX WITH BIOTIN (chains A) DPSKDSKAQVSAAEAGITGTWYNQLGSTFIVTAGADGALTGTYESAVGNAESRYVLTGRY DSAPATDGSGTALGWTVAWKNNYRNAHSATTWSGQYVGGAEARINTQWLLTSGTTEANAW KSTLVGHDTFTKVKPSAASIDAAKKAGVNNGNPLDAVQQ
| ID | Name | Formula | Copies |
|---|---|---|---|
| BTN | Biotin | C10 H16 N2 O3 S | 1 |
Structural origins of high-affinity biotin binding to streptavidin. Weber, P.C., Ohlendorf, D.H., Wendoloski, J.J. et al. Science (1989) 243:85-88. PubMed
Other PDB entries of the same protein (UniProt P22629 (AlphaFold model), which also has an AlphaFold model), best resolution first:
1STP is part of these collections:
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