› 2l9g

Solution NMR

Solution structure of AS1p-Tar in 10% negatively charged bicelles

Released:
DOI: 10.2210/pdb2l9g/pdb
PDB entry 2l9g coloured by chain, ensemble of 25 models, front view.
PDB entry 2l9g coloured by chain, ensemble of 25 models, side view.
PDB entry 2l9g coloured by chain, ensemble of 25 models, top view.
Source organism: Escherichia coli K-12
Primary publication:
Structural characterization of AS1-membrane interactions from a subset of HAMP domains.
Unnerståle S, Mäler L, Draheim RR
Biochim Biophys Acta 1808 2403-12 (2011)
PMID: 21763270

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139349 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Methyl-accepting chemotaxis protein II Chain: A
Molecule details ›
Chain: A
Length: 19 amino acids
Theoretical weight: 2.12 KDa
Source organism: Escherichia coli K-12
Expression system: Not provided
UniProt:
  • Canonical: P07017 (Residues: 214-232; Coverage: 3%)
Gene names: JW1875, b1886, cheM, tar
Sequence domains: HAMP domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 42%
Refinement method: molecular dynamics
Expression system: Not provided

Quick links

Citations

2 review citations

The magic of bicelles lights up membrane protein structure.
Dürr et al. (2012)
1 more

1 mention without citation

Structural characterization of AS1-membrane interactions from a subset of HAMP domains.
Unnerståle et al. (2011)