1rxk

X-ray diffraction
1.7Å resolution

crystal structure of streptavidin mutant (M3) a combination of M1+M2

Released:
Source organism: Streptomyces avidinii
Primary publication:
Structural elements responsible for conversion of streptavidin to a pseudoenzyme.
Proc. Natl. Acad. Sci. U.S.A. 101 5916-21 (2004)
PMID: 15079055

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Streptavidin Chains: A, B
Molecule details ›
Chains: A, B
Length: 125 amino acids
Theoretical weight: 13.33 KDa
Source organism: Streptomyces avidinii
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P22629 (Residues: 38-71, 72-159; Coverage: 77%)
Sequence domains: Avidin family
Structure domains: Avidin-like

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: C2221
Unit cell:
a: 80.335Å b: 81.579Å c: 90.532Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.213 0.2 0.239
Expression system: Escherichia coli BL21