Structural basis for maintenance of bacterial outer membrane lipid asymmetry

Structure

x-ray diffraction · 3 distinct chains.

Ligands and binding sites

• GP1 · 2-amino-2-deoxy-1-O-phosphono-alpha-D-glucopyranose · ligand · 3 copies · chains C, A, E
• Z9M · 2-amino-2-deoxy-4-O-phosphono-beta-D-glucopyranose · ligand · 3 copies · chains C, A, E
• KDO · 3-deoxy-alpha-D-manno-oct-2-ulopyranosonic acid · sugar · 5 copies · chains C, A, E
• CA · Calcium ion · metal · 3 copies · chains C, A, E
• SO4 · Sulfate ion · ion · 8 copies · chains C, E, A
• C8E · (hydroxyethyloxy)tri(ethyloxy)octane · additive · 3 copies · chains C, A, D, E

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Compared structures

• 5NUR · Structural basis for maintenance of bacterial outer membrane lipid asymmetry · the same entry in another collection · chain A against A, TM-score 1.00
• P02931 · AlphaFold monomer V2.0 prediction for outer membrane porin F (P02931) · a predicted model of the same protein · chain C against A, TM-score 1.00

Analyse

• Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
• Every structure of UniProt P02931
• Every structure of UniProt A0A0W8AQT6
• Elsewhere: RCSB PDB 5NUR · PDBe 5NUR · UniProt P02931 · UniProt A0A0W8AQT6