› 1mpq

X-ray diffraction
3Å resolution

MALTOPORIN TREHALOSE COMPLEX

Released:
DOI: 10.2210/pdb1mpq/pdb
PDB entry 1mpq coloured by chain, front view.
PDB entry 1mpq coloured by chain, side view.
PDB entry 1mpq coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Channel specificity: structural basis for sugar discrimination and differential flux rates in maltoporin.
Wang YF, Dutzler R, Rizkallah PJ, Rosenbusch JP, Schirmer T
J Mol Biol 272 56-63 (1997)
PMID: 9299337

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-136410 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Maltoporin Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 421 amino acids
Theoretical weight: 47.43 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P02943 (Residues: 26-446; Coverage: 100%)
Gene names: JW3996, b4036, lamB, malB
Sequence domains: LamB porin
Structure domains: Porin, LamB type

Ligands and Environments

Carbohydrate polymer : NEW Components: GLC
Carbohydrate polymer
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ELLIOTT GX-20
Spacegroup: C2221
Unit cell:
a: 130Å b: 212.2Å c: 218.2Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.218 0.218 0.241
Expression system: Escherichia coli

Quick links

Citations

14 review citations

Molecular basis of bacterial outer membrane permeability revisited.
Nikaido H. (2003)
13 more

3 mentions without citation

The structural biology of β-barrel membrane proteins: a summary of recent reports.
Fairman et al. (2011)
2 more