P63172: Dynein light chain Tctex-type 1 (DYNLT1)

Dynein light chain Tctex-type 1 (DYNLT1) is a 113-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P63172.

Gene
DYNLT1
Organism
Homo sapiens
Length
113 residues
Mean pLDDT
95.1
Model
AF-P63172-F1 v6
Model created
1 Aug 2025
PDB structures
14

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Model confidence (pLDDT)

The mean pLDDT of this model is 95.1 (very high 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 accurate91%
70 to 90Confident: backbone generally right5%
50 to 70Low: treat with caution4%
Below 50Very low: often disordered regions0%

What pLDDT means and how to read it

Function

Component of dynein, a family of motor proteins essential for movement along microtubules (By similarity). Required for structural and functional integrity of cilia (By similarity). 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. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. Binds to transport cargos and is involved in apical cargo transport such as rhodopsin-bearing vesicles in polarized epithelia

Subunit structure

Homodimer (Probable). 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…

Subcellular location

Golgi apparatus, Cytoplasm, Cytoplasm, cytoskeleton, spindle

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
8RGIX-ray2.02 ÅA=2-113
9BLYEM3.5 ÅK/L=1-113
8J07EM4.1 Ål8/n8/p8/r8=1-113
9E28EM4.4 Åk/v=1-113
9E12EM4.5 ÅK/L=1-113
9E13EM4.5 ÅK/L=1-113
9E14EM5.0 ÅK/L=1-113
9YNHEM5.5 ÅK/L=1-113
9E23EM6.2 Åk/v=1-113
8PR1EM8.2 ÅK/L=1-113
9YNEEM8.46 Åk/v=1-113
8PR0EM9.4 ÅG/H=1-113
8PTKEM10.0 Åk/l/v/y=1-113
5JPWNMRA/B=1-113

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