› 1n7y

X-ray diffraction
1.96Å resolution

STREPTAVIDIN MUTANT N23E AT 1.96A

Released:
DOI: 10.2210/pdb1n7y/pdb
PDB entry 1n7y coloured by chain, front view.
PDB entry 1n7y coloured by chain, side view.
PDB entry 1n7y coloured by chain, top view.
Source organism: Streptomyces avidinii
Primary publication:
Structural studies of hydrogen bonds in the high-affinity streptavidin-biotin complex: mutations of amino acids interacting with the ureido oxygen of biotin.
Le Trong I, Freitag S, Klumb LA, Chu V, Stayton PS, Stenkamp RE
Acta Crystallogr D Biol Crystallogr 59 1567-73 (2003)
PMID: 12925786

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: 13.3 KDa
Source organism: Streptomyces avidinii
Expression system: Escherichia coli BL21
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
Spacegroup: P21
Unit cell:
a: 58.3Å b: 87.7Å c: 46.8Å
α: 90° β: 98.9° γ: 90°
R-values:
R R work R free
0.186 0.182 0.284
Expression system: Escherichia coli BL21

Quick links

Citations

1 review citation

Catalytic robustness and torque generation of the F1-ATPase.
Noji et al. (2017)
11 other articles