Pfam | PF02271 Ubiquinol-cytochrome C reductase complex 14kD subunit

UCR_14kD


Sequence View

The following plot shows contacts with headgroups (magenta), acyl tails (yellow/orange) and solvent (blue) from simulations of 55 protein structures including this sequence. You can choose between showing only consensus values (based on a mean of all structures) and showing data from all structures. If data from all structures is shown, you can click on a residue to view more information.

Secondary structure is also shown using blue for alpha helices and green for beta strands. More conserved residues are indicated by darker coloured areas of secondary structure. Secondary structure which is not conserved in at least 50% of aligned residues is not shown. Domains which are identified through simulation to exist inside the bilayer are indicated by shaded boxes around the secondary structure. The shading of the box indicates the depth within the bilayer, from shallow (red) to deep (yellow).

Alignment of UniProt sequences was carried out using MUSCLE. Displayed sequence is a consensus derived from the alignment.


QSFTSIARIGDYILVSASSRWLEGIRKWYYNAAGFNKLGLMRDDTIHENDNDVKEAIRRLPENLYDDRVFRIKRALDLSMRQQILPKEQWTKYEEDKSYLEPYLKEVIRERKEREEWAKK
102030405060708090100110120

I

Statistics

Shown below are histograms for all MemProtMD entries in grey and for this collection only in blue. Densities for all entries and for this collection are individually normalised. Publication date, resolution and experimental_method are taken directly from the PDB record, whilst membrane thickness is derived from MemProtMD simulations.

Publication date

1990199520002005201020152020

Experimental method

ELECTRON CRYSTALLOGRAPHY ELECTRON MICROSCOPY FIBER DIFFRACTION FIBER DIFFRACTION, SOLID-STATE SOLID-STATE SOLUTION SOLUTION NMR, SOLID-STATE X-RAY DIFFRACTION X-RAY DIFFRACTION,

Resolution

0.00.51.01.52.02.53.03.54.04.55.05.5

Membrane thickness

2224262830323436384042