Q9D6K9: Ceramide synthase 5 (Cers5)

Ceramide synthase 5 (Cers5) is a 414-residue protein from Mus musculus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9D6K9.

Gene
Cers5
Organism
Mus musculus
Length
414 residues
Mean pLDDT
82.1
Model
AF-Q9D6K9-F1 v6
Model created
1 Aug 2025
PDB structures
4

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Model confidence (pLDDT)

The mean pLDDT of this model is 82.1 (confident overall). pLDDT is AlphaFold's per-residue confidence score from 0 to 100. In MolViewer, choose the B-factor color scheme to color the model by pLDDT, because AlphaFold stores it in the B-factor column.

pLDDT bandMeaningShare of residues
Above 90Very high: backbone and side chains are usually accurate64%
70 to 90Confident: backbone generally right16%
50 to 70Low: treat with caution3%
Below 50Very low: often disordered regions17%

What pLDDT means and how to read it

Function

Ceramide synthase that catalyzes the transfer of the fatty acyl chain from fatty acyl-CoA to a sphingoid base, with high selectivity toward palmitoyl-CoA (hexadecanoyl-CoA; C16:0-CoA) (PubMed:12912983, PubMed:15823095, PubMed:16100120, PubMed:17609214, PubMed:17977534, PubMed:26853464, PubMed:38961186). Can use different sphingoid bases as substrates for ceramide synthesis, such as sphinganine in de novo synthesis, and sphing-4E-enine (sphingosine), (4R)-hydroxysphinganine (phytosphingosine) or sphinga-4E,14Z-dienine in salvage pathways (By similarity) (PubMed:12912983, PubMed:15772421, PubMed:15823095, PubMed:17977534). Other fatty acyl-CoAs such as long-chain saturated stearoyl-CoA…

Subunit structure

Interacts with PAQR4; the interaction regulates the stability and activity of CERS5 and is inhibited in presence of ceramides

Subcellular location

Endoplasmic reticulum membrane

Experimental structures in the PDB

Compare the prediction with experimentally determined structures of the same protein:

PDB IDMethodResolutionChains and residues
5E8OX-ray1.98 ÅC/F=379-387
5E8PX-ray2.0 ÅC/F=379-387
5E8NX-ray2.25 ÅC/F/I/L=379-387
2CQXNMRA=77-135

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