Q9NP97: Dynein light chain roadblock-type 1 (DYNLRB1)

Dynein light chain roadblock-type 1 (DYNLRB1) is a 96-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9NP97.

Gene
DYNLRB1
Organism
Homo sapiens
Length
96 residues
Mean pLDDT
93.2
Model
AF-Q9NP97-F1 v6
Model created
1 Aug 2025
PDB structures
24

Explore in 3D Color by confidence AlphaFold DB UniProt

Model confidence (pLDDT)

The mean pLDDT of this model is 93.2 (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 accurate89%
70 to 90Confident: backbone generally right10%
50 to 70Low: treat with caution1%
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 (Probable). Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules (Probable)

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

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
2HZ5X-ray2.1 ÅA/B=1-96
6F1ZEM3.4 Ås/t=1-96
6F1TEM3.5 Åk/l/s/t=1-96
9BLYEM3.5 ÅG/H=1-96
6SC2EM3.9 ÅG/H=1-96
8RGHEM3.9 ÅG/H=1-96
8RGGEM4.0 ÅG/H=1-96
8J07EM4.1 Åk4/m4/o4/q4=1-96
9E28EM4.4 ÅE/F=1-96
6RLBEM4.5 ÅG/H=1-96
9E12EM4.5 ÅG/H=1-96
9E13EM4.5 ÅG/H=1-96
9E14EM5.0 ÅG/H=1-96
9YNHEM5.5 ÅG/H=1-96
9E23EM6.2 ÅE/F=1-96
9HHLEM6.53 Ås/t/w/z=1-96
6F38EM6.7 Åk/l/s/t=1-96
6F3AEM8.2 Åk/l=1-96
8PR1EM8.2 Ås/t=1-96
8PTKEM10.0 Ås/t/w/z=1-96

Showing 20 of 24 experimental structures (best resolution first).

More AlphaFold highlights

About this viewer

MolViewer loads the AlphaFold model straight from AlphaFold DB into your browser. Show it as a cartoon, color by pLDDT, measure distances and angles, and load a PDB structure next to it to compare.