A0A5G2QD80: Dynactin subunit 2 (DCTN2)

Dynactin subunit 2 (DCTN2) is a 405-residue protein from Sus scrofa. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: A0A5G2QD80.

Gene
DCTN2
Organism
Sus scrofa
Length
405 residues
Mean pLDDT
74.1
Model
AF-A0A5G2QD80-F1 v6
Model created
1 Aug 2025
PDB structures
22

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Model confidence (pLDDT)

The mean pLDDT of this model is 74.1 (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 accurate29%
70 to 90Confident: backbone generally right31%
50 to 70Low: treat with caution30%
Below 50Very low: often disordered regions10%

What pLDDT means and how to read it

Function

Part of the dynactin complex that activates the molecular motor dynein for ultra-processive transport along microtubules. In the dynactin soulder domain, binds the ACTR1A filament and acts as a molecular ruler to determine the length (PubMed:25814576, PubMed:29420470, PubMed:33734450, PubMed:36071160). Modulates cytoplasmic dynein binding to an organelle, and plays a role in prometaphase chromosome alignment and spindle organization during mitosis. Involved in anchoring microtubules to centrosomes. May play a role in synapse formation during brain development (By similarity)

Subunit structure

Subunit of dynactin, a multiprotein complex part of a tripartite complex with dynein and a adapter, such as BICDL1, BICD2 or HOOK3 (PubMed:25814576, PubMed:29420470, PubMed:33734450, PubMed:36071160). The dynactin complex is built around ACTR1A/ACTB filament and consists of an actin-related filament composed of a shoulder domain, a pointed end and a barbed end. Its length is defined by its…

Subcellular location

Cytoplasm, cytoskeleton, Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, Membrane

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
7Z8MEM3.37 ÅM=1-405
6F1UEM3.4 Åc=1-50, d=1-26
5AFUEM3.5 Åa=1-48
6F1TEM3.5 Åa=1-66, b=1-89, c=1-50, d=1-26
6ZNLEM3.8 ÅM/N/m/n=1-405
9DGSEM3.9 ÅM/N/P/Q=1-405
5ADXEM4.0 Åa=1-48
9YNGEM4.07 ÅM/N/P/Q=1-405
6ZNMEM4.1 ÅM=1-405
6ZNNEM4.5 ÅM=1-405
9HHLEM6.53 ÅM/N/P/Q/V=1-405
6F38EM6.7 Åa=1-68, b=1-90, d=1-29
6ZNOEM6.8 ÅM=1-405
9DGUEM7.1 ÅM/N/P/Q=1-405
9DGTEM7.2 ÅM/N/P/Q=1-405
6F3AEM8.2 Åa=1-68, b/c/d=1-89
6ZO4EM8.2 ÅM=1-405
5NW4EM8.7 Åk=1-64
9DGVEM8.8 ÅM/N/P/Q=1-405
8PTKEM10.0 ÅM/N/P/Q=1-405

Showing 20 of 22 experimental structures (best resolution first).

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