› 2mpr

X-ray diffraction
2.4Å resolution

MALTOPORIN FROM SALMONELLA TYPHIMURIUM

Released:
DOI: 10.2210/pdb2mpr/pdb
PDB entry 2mpr coloured by chain, front view.
PDB entry 2mpr coloured by chain, side view.
PDB entry 2mpr coloured by chain, top view.
Source organism: Salmonella enterica subsp. enterica serovar Typhimurium
Primary publication:
Structure of maltoporin from Salmonella typhimurium ligated with a nitrophenyl-maltotrioside.
Meyer JE, Hofnung M, Schulz GE
J Mol Biol 266 761-75 (1997)
PMID: 9102468

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-150758 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Maltoporin Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 427 amino acids
Theoretical weight: 48.06 KDa
Source organism: Salmonella enterica subsp. enterica serovar Typhimurium
UniProt:
  • Canonical: P26466 (Residues: 26-452; Coverage: 100%)
Gene names: STM4231, lamB, malL
Sequence domains: LamB porin
Structure domains: Porin, LamB type

Ligands and Environments

Carbohydrate polymer : NEW Components: BGC, GLC
Carbohydrate polymer
1 bound ligand:
Ligand CA 1 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MACSCIENCE M18X
Spacegroup: C2221
Unit cell:
a: 124.5Å b: 211.8Å c: 184.3Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.191 0.191 0.222

Quick links

Citations

17 review citations

Membrane protein folding and stability: physical principles.
White et al. (1999)
16 more

19 mentions without citation

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