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› 4nh2

X-ray diffraction
2.3Å resolution

Crystal structure of AmtB from E. coli bound to phosphatidylglycerol

Released:
DOI: 10.2210/pdb4nh2/pdb
PDB entry 4nh2 coloured by chain, front view.
PDB entry 4nh2 coloured by chain, side view.
PDB entry 4nh2 coloured by chain, top view.
Source organism: Escherichia coli BL21(DE3)
Primary publication:
Membrane proteins bind lipids selectively to modulate their structure and function.
Laganowsky A, Reading E, Allison TM, Ulmschneider MB, Degiacomi MT, Baldwin AJ, Robinson CV
OpenAccess logo Nature 510 172-175 (2014)
PMID: 24899312

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-164891 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ammonia channel Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 406 amino acids
Theoretical weight: 42.3 KDa
Source organism: Escherichia coli BL21(DE3)
Expression system: Escherichia coli
Structure domains: Ammonium transporter AmtB like domains

Ligands and Environments

1 bound ligand:
Ligand P6L 8 x P6L
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: C2221
Unit cell:
a: 116.19Å b: 201.19Å c: 232.45Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.203 0.202 0.234
Expression system: Escherichia coli

Quick links

Citations

105 review citations

The mystery of membrane organization: composition, regulation and roles of lipid rafts.
Sezgin et al. (2017)
104 more

13 mentions without citation

Membrane proteins bind lipids selectively to modulate their structure and function.
Laganowsky et al. (2014)
12 more