› 1mm9

X-ray diffraction
1.66Å resolution

Streptavidin Mutant with Insertion of Fibronectin Hexapeptide, including RGD

Released:
DOI: 10.2210/pdb1mm9/pdb
PDB entry 1mm9 coloured by chain, front view.
PDB entry 1mm9 coloured by chain, side view.
PDB entry 1mm9 coloured by chain, top view.
Source organism: Streptomyces avidinii
Primary publication:
Structural characterization and comparison of RGD cell-adhesion recognition sites engineered into streptavidin.
Le Trong I, McDevitt TC, Nelson KE, Stayton PS, Stenkamp RE
Acta Crystallogr D Biol Crystallogr 59 828-34 (2003)
PMID: 12777798

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assemblies composition:
homo tetramer
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149691 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Streptavidin Chain: A
Molecule details ›
Chain: A
Length: 130 amino acids
Theoretical weight: 13.56 KDa
Source organism: Streptomyces avidinii
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P22629 (Residues: 37-88, 92-163; Coverage: 78%)
Sequence domains: Avidin family
Structure domains: Avidin-like

Ligands and Environments

1 bound ligand:
Ligand MRD 2 x MRD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-1
Spacegroup: I4122
Unit cell:
a: 56.9Å b: 56.9Å c: 170.8Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.145 0.134 0.195
Expression system: Escherichia coli BL21

Quick links

Citations

1 review citation

Osteopontin: an effector and an effect of tumor metastasis.
Shevde et al. (2010)
6 other articles

2 mentions without citation

Second-contact shell mutation diminishes streptavidin-biotin binding affinity through transmitted effects on equilibrium dynamics.
Baugh et al. (2012)
1 more