› 1mal

X-ray diffraction
3.1Å resolution

STRUCTURAL BASIS FOR SUGAR TRANSLOCATION THROUGH MALTOPORIN CHANNELS AT 3.1 ANGSTROMS RESOLUTION

Released:
DOI: 10.2210/pdb1mal/pdb
PDB entry 1mal coloured by chain, front view.
PDB entry 1mal coloured by chain, side view.
PDB entry 1mal coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structural basis for sugar translocation through maltoporin channels at 3.1 A resolution.
Schirmer T, Keller TA, Wang YF, Rosenbusch JP
Science 267 512-4 (1995)
PMID: 7824948

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
Macromolecule:
Maltoporin Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 421 amino acids
Theoretical weight: 47.43 KDa
Source organism: 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

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: C2221
Unit cell:
a: 131.89Å b: 214.79Å c: 220.19Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.217 0.217 0.24

Quick links

Citations

72 review citations

The bacterial cell envelope.
Silhavy et al. (2010)
71 more

20 mentions without citation

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