› 1nl5

X-ray diffraction
2.1Å resolution

Engineered High-affinity Maltose-Binding Protein

Released:
DOI: 10.2210/pdb1nl5/pdb
PDB entry 1nl5 coloured by chain, front view.
PDB entry 1nl5 coloured by chain, side view.
PDB entry 1nl5 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
Macromolecules (2 distinct):
Maltose/maltodextrin-binding periplasmic protein Chain: A
Molecule details ›
Chain: A
Length: 366 amino acids
Theoretical weight: 40.1 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

Carbohydrate polymer : NEW Components: GLC
Carbohydrate polymer
1 bound ligand:
Ligand ZN 1 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P43212
Unit cell:
a: 121.59Å b: 121.59Å c: 62.44Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.252 0.252 0.29
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

5 mentions without citation

Protein Design: From the Aspect of Water Solubility and Stability.
Qing et al. (2022)
4 more