Pfam | PF04648 Yeast mating factor alpha hormone

MF_alpha


Sequence View

The following plot shows contacts with headgroups (magenta), acyl tails (yellow/orange) and solvent (blue) from simulations of 1 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.


WHWLQLKPGQPMY
10

Simulation 7ad3_default_dppc

Images

The following pre-rendered images show: distortions of the lipid bilayer, averaged across the entire simulation; positions of lipids in a representative snapshot of the simulation and contacts between lipids or solvent and the protein in either cartoon or surface representation. Rendering is performed using VMD's Tachyon renderer.

Distortions

Distortions show the average surface formed by lipid phosphate beads over the final 800 ns of simulation time. Red indicates a thinning of the bilayer (compared to bulk thickness), whilst blue indicates thickening.

Lipids

Coarse-grained lipids are shown with glycerol beads in yellow, phosphate beads in red and choline beads in blue. Atomistic lipids are coloured according to the CPK standard.

Contacts

Contacts show the average occupancy of the selected group within 6 Å of the protein over the final 800 ns of simulation time. Use the buttons below to select a representation.

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Polypeptide chains

Select a chain to view more detailed analysis. The cards below show a vertical violin plot for each chain, with shapes representing the normalised density of all residues (white), alpha helical residues (blue) and beta sheet residues (green) along the bilayer normal.

Chain A
Chain B
Chain E
Chain F
Chain G
Chain H
Chain I
Chain K