Q27974: Auxilin (DNAJC6)

Auxilin (DNAJC6) is a 910-residue protein from Bos taurus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q27974.

Gene
DNAJC6
Organism
Bos taurus
Length
910 residues
Mean pLDDT
63.0
Model
AF-Q27974-F1 v6
Model created
1 Aug 2025
PDB structures
9

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Model confidence (pLDDT)

The mean pLDDT of this model is 63.0 (low 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 accurate29%
70 to 90Confident: backbone generally right17%
50 to 70Low: treat with caution7%
Below 50Very low: often disordered regions48%

What pLDDT means and how to read it

Function

May act as a protein phosphatase and/or a lipid phosphatase (Probable). Co-chaperone that recruits HSPA8/HSC70 to clathrin-coated vesicles (CCVs) and promotes the ATP-dependent dissociation of clathrin from CCVs and participates in clathrin-mediated endocytosis of synaptic vesicles and their recycling and also in intracellular trafficking (PubMed:11470803, PubMed:8524399). Firstly, binds tightly to the clathrin cages, at a ratio of one DNAJC6 per clathrin triskelion (PubMed:15023062, PubMed:15502813, PubMed:21482805, PubMed:7705342, PubMed:8524399). The HSPA8:ATP complex then binds to the clathrin-auxilin cage, initially at a ratio of one HSPA8 per triskelion leading to ATP hydrolysis…

Subunit structure

Forms a complex composed of HSPA8, CLTC and DNAJC6 (PubMed:8524399). Interacts with HSPA8/HSC70 in an ATP-dependent manner; this interaction stimulates the HSPA8's ATPase activity (PubMed:12741832, PubMed:17996706). Interacts with CLTC; this interaction produces a local change in heavy-chain contacts, creating a detectable global distortion of the clathrin coat (PubMed:11470803, PubMed:15023062,…

Subcellular location

Cytoplasmic vesicle, clathrin-coated vesicle

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
2QWOX-ray1.7 ÅB=813-904
2QWPX-ray1.75 ÅB=813-904
3N0AX-ray2.2 ÅA=40-400
2QWQX-ray2.21 ÅB=813-904
2QWRX-ray2.21 ÅB=813-904
2QWNX-ray2.4 ÅB=812-905
1NZ6X-ray2.5 ÅA/B=810-910
1XI5EM12.0 ÅJ/K/L/M/N/O/P/Q/R=797-910
1N4CNMRA=737-910

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