Q8WVS4: Cytoplasmic dynein 2 intermediate chain 1 (DYNC2I1)

Cytoplasmic dynein 2 intermediate chain 1 (DYNC2I1) is a 1066-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q8WVS4.

Gene
DYNC2I1
Organism
Homo sapiens
Length
1066 residues
Mean pLDDT
63.5
Model
AF-Q8WVS4-F1 v6
Model created
1 Aug 2025
PDB structures
4

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Model confidence (pLDDT)

The mean pLDDT of this model is 63.5 (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 accurate27%
70 to 90Confident: backbone generally right21%
50 to 70Low: treat with caution15%
Below 50Very low: often disordered regions38%

What pLDDT means and how to read it

Function

Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 2 complex (dynein-2 complex), a motor protein complex that drives the movement of cargos along microtubules within cilia and flagella in concert with the intraflagellar transport (IFT) system (PubMed:23910462, PubMed:25205765, PubMed:29742051, PubMed:31451806). DYNC2I1 plays a major role in retrograde ciliary protein trafficking in cilia and flagella (PubMed:29742051, PubMed:30320547, PubMed:30649997). Also requires to maintain a functional transition zone (PubMed:30320547)

Subunit structure

Intermediate chain of the cytoplasmic dynein complex 2, a multisubunit complex, composed at least of eleven different proteins (PubMed:25205765, PubMed:31451806). The cytoplasmic dynein 2 complex consists of two catalytic heavy chains (HCs) and a number of non-catalytic subunits presented by intermediate chains (ICs), light intermediate chains (LICs) and light chains (LCs). Among them, a heavy…

Subcellular location

Cell projection, cilium, Cytoplasm, cytoskeleton, microtubule organizing center, centrosome

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
6SC2EM3.9 ÅC=1-1066
8RGHEM3.9 ÅC=1-1066
8RGGEM4.0 ÅC=1-1066
6RLBEM4.5 ÅC=1-1066

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