› 1kl4

X-ray diffraction
1.7Å resolution

AN ENGINEERED STREPTAVIDIN WITH IMPROVED AFFINITY FOR THE STREP-TAG II PEPTIDE : apo-SAM2

Released:
DOI: 10.2210/pdb1kl4/pdb
PDB entry 1kl4 coloured by chain, front view.
PDB entry 1kl4 coloured by chain, side view.
PDB entry 1kl4 coloured by chain, top view.
Source organism: Streptomyces avidinii
Primary publication:
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 IP, Skerra A
Protein Sci 11 883-93 (2002)
PMID: 11910031

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: 13.35 KDa
Source organism: Streptomyces avidinii
Expression system: Escherichia coli
UniProt:
  • Canonical: P22629 (Residues: 38-163; Coverage: 79%)
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 RU300
Spacegroup: P21
Unit cell:
a: 58.45Å b: 86.814Å c: 47.084Å
α: 90° β: 98.82° γ: 90°
R-values:
R R work R free
0.193 0.191 0.228
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Recombinant protein expression and purification: a comprehensive review of affinity tags and microbial applications.
Young et al. (2012)
4 more

2 mentions 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)
1 more