› 2o5x

X-ray diffraction
2.05Å resolution

Crystal structure of 1E9 LeuH47Trp/ArgH100Trp, an engineered Diels-Alderase Fab with nM steroid-binding affinity

Released:
DOI: 10.2210/pdb2o5x/pdb
PDB entry 2o5x coloured by chain, front view.
PDB entry 2o5x coloured by chain, side view.
PDB entry 2o5x coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Closely related antibody receptors exploit fundamentally different strategies for steroid recognition.
Verdino P, Aldag C, Hilvert D, Wilson IA
Proc Natl Acad Sci U S A 105 11725-30 (2008)
PMID: 18689687

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
hetero dimer (preferred)
hetero tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-213161 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
chimeric antibody Fab 1E9-DB3 Chain: L
Molecule details ›
Chain: L
Length: 219 amino acids
Theoretical weight: 24.14 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
Structure domains: Immunoglobulins
chimeric antibody Fab 1E9-DB3 Chain: H
Molecule details ›
Chain: H
Length: 227 amino acids
Theoretical weight: 24.43 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
Structure domains: Immunoglobulins

Ligands and Environments

2 bound ligands:
Ligand SO4 11 x SO4
Ligand TRS 1 x TRS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.1
Spacegroup: P3121
Unit cell:
a: 127.573Å b: 127.573Å c: 91.928Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.179 0.178 0.204
Expression system: Escherichia coli

Quick links

Citations

3 citation in other articles

High-Affinity Nucleic-Acid-Based Receptors for Steroids.
Yang et al. (2017)
2 more

1 mention without citation

Closely related antibody receptors exploit fundamentally different strategies for steroid recognition.
Verdino et al. (2008)