1stp

X-ray diffraction
2.6Å resolution

STRUCTURAL ORIGINS OF HIGH-AFFINITY BIOTIN BINDING TO STREPTAVIDIN

Released:

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:

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:
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