› 2mnh

Solution NMR

Refined structure of outer membrane protein x in nanodisc by measuring residual dipolar couplings

Released:
DOI: 10.2210/pdb2mnh/pdb
PDB entry 2mnh coloured by chain, ensemble of 10 models, front view.
PDB entry 2mnh coloured by chain, ensemble of 10 models, side view.
PDB entry 2mnh coloured by chain, ensemble of 10 models, top view.
Source organism: Escherichia coli str. K-12 substr. MC4100
Primary publication:
Measuring membrane protein bond orientations in nanodiscs via residual dipolar couplings.
Bibow S, Carneiro MG, Sabo TM, Schwiegk C, Becker S, Riek R, Lee D
Protein Sci 23 851-6 (2014)
PMID: 24752984

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141785 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Outer membrane protein X Chain: A
Molecule details ›
Chain: A
Length: 148 amino acids
Theoretical weight: 16.37 KDa
Source organism: Escherichia coli str. K-12 substr. MC4100
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0A917 (Residues: 24-171; Coverage: 100%)
Gene names: JW0799, b0814, ompX, ybiG
Sequence domains: Outer membrane protein beta-barrel domain
Structure domains: Porin

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 15%
Refinement method: simulated annealing
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

4 review citations

Recent advances in nanodisc technology for membrane protein studies (2012-2017).
Rouck et al. (2017)
3 more

4 mentions without citation

Solution NMR: A powerful tool for structural and functional studies of membrane proteins in reconstituted environments.
Puthenveetil et al. (2019)
3 more