› 1n4j

X-ray diffraction
2.18Å resolution

STREPTAVIDIN MUTANT N23A AT 2.18A

Released:
DOI: 10.2210/pdb1n4j/pdb
Model geometry
Fit model/data
PDB entry 1n4j coloured by chain, front view.
PDB entry 1n4j coloured by chain, side view.
PDB entry 1n4j 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 Chain: A
Molecule details ›
Chain: A
Length: 127 amino acids
Theoretical weight: 13.24 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

wwPDB Validation report is not available for this entry.
X-ray source: SIEMENS
Spacegroup: I4122
Unit cell:
a: 59.2Å b: 59.2Å c: 179.8Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.188 0.188 0.253
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

1 mention without citation

The high-intensity option of the SANS diffractometer KWS-2 at JCNS - characterization and performance of the new multi-megahertz detection system.
Houston et al. (2018)