› 1stp

X-ray diffraction
2.6Å resolution

STRUCTURAL ORIGINS OF HIGH-AFFINITY BIOTIN BINDING TO STREPTAVIDIN

Released:
DOI: 10.2210/pdb1stp/pdb
PDB 1stp coloured by chain and viewed from the front.
PDB 1stp coloured by chain and viewed from the side.
PDB 1stp coloured by chain and viewed from the top.
Source organism: Streptomyces avidinii
Primary publication:
Structural origins of high-affinity biotin binding to streptavidin.
Weber PC, Ohlendorf DH, Wendoloski JJ, Salemme FR
Science 243 85-8 (1989)
PMID: 2911722

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Streptavidin Chain: A
Molecule details ›
Chain: A
Length: 159 amino acids
Theoretical weight: 16.5 KDa
Source organism: Streptomyces avidinii
Expression system: Not provided
UniProt:
  • Canonical: P22629 (Residues: 25-183; Coverage: 100%)
Structure domains: Avidin-like

Ligands and Environments

1 bound ligand:
Ligand BTN 1 x BTN
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: I4122
Unit cell:
a: 99.4Å b: 99.4Å c: 125.8Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.22 not available not available
Expression system: Not provided

Quick links

Citations

44 review citations

Immobilization Techniques for Aptamers on Gold Electrodes for the Electrochemical Detection of Proteins: A Review.
Oberhaus et al. (2020)
43 more

33 mentions without citation

Intrinsic tryptophan fluorescence in the detection and analysis of proteins: a focus on Förster resonance energy transfer techniques.
Ghisaidoobe et al. (2014)
32 more