› 3nog

X-ray diffraction
3.34Å resolution

Designed ankyrin repeat protein (DARPin) Binders to AcrB: Plasticity of the Interface

Released:
DOI: 10.2210/pdb3nog/pdb
PDB entry 3nog coloured by chain, front view.
PDB entry 3nog coloured by chain, side view.
PDB entry 3nog coloured by chain, top view.
Source organisms:
Primary publication:
Designed ankyrin repeat protein binders for the crystallization of AcrB: plasticity of the dominant interface.
Monroe N, Sennhauser G, Seeger MA, Briand C, Grütter MG
J Struct Biol 174 269-81 (2011)
PMID: 21296164

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero pentamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151930 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Multidrug efflux pump subunit AcrB Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 1049 amino acids
Theoretical weight: 113.69 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P31224 (Residues: 1-1049; Coverage: 100%)
Gene names: JW0451, acrB, acrE, b0462
Sequence domains: AcrB/AcrD/AcrF family
Structure domains:
Designed ankyrin repeat protein Chains: D, E
Molecule details ›
Chains: D, E
Length: 169 amino acids
Theoretical weight: 18.2 KDa
Source organism: synthetic construct
Expression system: Escherichia coli
Structure domains: Ankyrin repeat-containing domain

Ligands and Environments

No bound ligands
1 modified residue:
Ligand FME 3 x FME

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P212121
Unit cell:
a: 145.4Å b: 158Å c: 258.6Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.258 0.257 0.308
Expression system: Escherichia coli

Quick links

Citations

2 review citations

New concepts and aids to facilitate crystallization.
Bukowska et al. (2013)
1 more

7 mentions without citation

Structural insights for engineering binding proteins based on non-antibody scaffolds.
Gilbreth et al. (2012)
6 more