Q13409: Cytoplasmic dynein 1 intermediate chain 2 (DYNC1I2)

Cytoplasmic dynein 1 intermediate chain 2 (DYNC1I2) is a 638-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q13409.

Gene
DYNC1I2
Organism
Homo sapiens
Length
638 residues
Mean pLDDT
72.7
Model
AF-Q13409-F1 v6
Model created
1 Aug 2025
PDB structures
29

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Model confidence (pLDDT)

The mean pLDDT of this model is 72.7 (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 accurate17%
70 to 90Confident: backbone generally right52%
50 to 70Low: treat with caution10%
Below 50Very low: often disordered regions22%

What pLDDT means and how to read it

Function

Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function (PubMed:31079899). Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules (PubMed:31079899). The intermediate chains mediate the binding of dynein to dynactin via its 150 kDa component (p150-glued) DCTN1 (By similarity). Involved in membrane-transport, such as Golgi apparatus, late endosomes and lysosomes (By similarity)

Subunit structure

Homodimer. The cytoplasmic dynein 1 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); the composition seems to vary in respect to the IC, LIC and LC composition. The heavy chain homodimer serves as a scaffold for the probable homodimeric assembly of the…

Subcellular location

Cytoplasm, cytoskeleton, Cytoplasm

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
7Z8IEM3.3 Åh/o=1-638
6F1UEM3.4 Åh=1-638
6F1ZEM3.4 Åo/p=1-638
6F1TEM3.5 Åg/h/o/p=1-638
9BLYEM3.5 ÅC/D=1-638
8PR2EM3.8 Åh=1-638
8PR3EM3.9 Åh/o=1-638
7Z8JEM3.93 Åh/o=1-638
9YNCEM3.93 ÅG/H=1-638
9YNGEM4.07 Åg/h/o/p=1-638
8PQWEM4.2 ÅH/I=1-638
9YNDEM4.26 ÅF/G=1-638
7Z8KEM4.37 Åh=72-638
9E28EM4.4 ÅD/H/g/h=1-638
9E12EM4.5 ÅC/D=1-638
9E13EM4.5 ÅC/D=1-638
9E14EM5.0 ÅC/D=1-638
8PQZEM5.5 ÅH/I=1-638
9YNHEM5.5 ÅC/D/U/V=1-638
9E23EM6.2 ÅD/H/g/h=1-638

Showing 20 of 29 experimental structures (best resolution first).

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