› 1swh

X-ray diffraction
1.7Å resolution

CORE-STREPTAVIDIN MUTANT W79F AT PH 4.5

Released:
DOI: 10.2210/pdb1swh/pdb
PDB entry 1swh coloured by chain, front view.
PDB entry 1swh coloured by chain, side view.
PDB entry 1swh coloured by chain, top view.
Source organism: Streptomyces avidinii
Primary publication:
Structural studies of binding site tryptophan mutants in the high-affinity streptavidin-biotin complex.
Freitag S, Le Trong I, Chilkoti A, Klumb LA, Stayton PS, Stenkamp RE
J Mol Biol 279 211-21 (1998)
PMID: 9636711

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
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 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 127 amino acids
Theoretical weight: 13.24 KDa
Source organism: Streptomyces avidinii
Expression system: Escherichia coli
UniProt:
  • Canonical: P22629 (Residues: 37-163; Coverage: 80%)
Sequence domains: Avidin family
Structure domains: Avidin-like

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P21
Unit cell:
a: 58.3Å b: 86.7Å c: 46.9Å
α: 90° β: 98.8° γ: 90°
R-values:
R R work R free
0.166 not available 0.244
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Streptavidin-biotin binding energetics.
Stayton et al. (1999)
1 more

1 mention without citation

Improved affinity of engineered streptavidin for the Strep-tag II peptide is due to a fixed open conformation of the lid-like loop at the binding site.
Korndörfer et al. (2002)