1STP: Streptavidin complex with biotin

Structural origins of high-affinity biotin binding to streptavidin. Determined by X-ray diffraction at 2.6 Å resolution. Released 15 Oct 1992.

Method
X-ray diffraction
Resolution
2.6 Å
Organism
Streptomyces avidinii
Chains
1
Atoms
1,001
Mol. weight
16.75 kDa
Ligands
BTN
Released
15 Oct 1992

Explore 1STP in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 3 helices, 8 β-strands

ElementResiduesLengthSheet
α-helix14-174
β-strand19-2351
β-strand28-3361
β-strand38-4471
β-strand54-6071
α-helix69-702
β-strand71-80101
β-strand85-97131
β-strand103-112101
α-helix116-1216
β-strand123-13191

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Streptavidin complex with biotinAprotein159Streptomyces avidiniiP22629 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1STP_1 STREPTAVIDIN COMPLEX WITH BIOTIN (chains A)
DPSKDSKAQVSAAEAGITGTWYNQLGSTFIVTAGADGALTGTYESAVGNAESRYVLTGRY
DSAPATDGSGTALGWTVAWKNNYRNAHSATTWSGQYVGGAEARINTQWLLTSGTTEANAW
KSTLVGHDTFTKVKPSAASIDAAKKAGVNNGNPLDAVQQ

Ligands and cofactors

IDNameFormulaCopies
BTNBiotinC10 H16 N2 O3 S1

Primary citation

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:

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