› 1stp

X-ray diffraction
2.6Å resolution

STRUCTURAL ORIGINS OF HIGH-AFFINITY BIOTIN BINDING TO STREPTAVIDIN

Released:
DOI: 10.2210/pdb1stp/pdb
PDB entry 1stp coloured by chain, front view.
PDB entry 1stp coloured by chain, side view.
PDB entry 1stp coloured by chain, top view.
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)
Assembly name:
PDBe Complex ID:
PDB-CPX-149694 (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%)
Sequence domains: Avidin family
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

50 review citations

Integrated nanoparticle-biomolecule hybrid systems: synthesis, properties, and applications.
Katz et al. (2004)
49 more

56 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)
55 more