› 1n3x

X-ray diffraction
2.5Å resolution

Ligand-free High-Affinity Maltose-Binding Protein

Released:
DOI: 10.2210/pdb1n3x/pdb
PDB entry 1n3x coloured by chain, front view.
PDB entry 1n3x coloured by chain, side view.
PDB entry 1n3x coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Insights into the conformational equilibria of maltose-binding protein by analysis of high affinity mutants.
Telmer PG, Shilton BH
J Biol Chem 278 34555-67 (2003)
PMID: 12794084

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142613 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Maltose/maltodextrin-binding periplasmic protein Chain: A
Molecule details ›
Chain: A
Length: 366 amino acids
Theoretical weight: 40.22 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0AEX9 (Residues: 27-396; Coverage: 99%)
Gene names: JW3994, b4034, malE
Sequence domains: Bacterial extracellular solute-binding protein
Structure domains: Periplasmic binding protein-like II

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P21
Unit cell:
a: 44.59Å b: 71.33Å c: 59.01Å
α: 90° β: 101.53° γ: 90°
R-values:
R R work R free
0.197 0.197 0.241
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Structure, function, and evolution of bacterial ATP-binding cassette systems.
Davidson et al. (2008)
5 more

4 mentions without citation

Visualizing conformational dynamics of proteins in solution and at the cell membrane.
Gordon et al. (2018)
3 more