Q15078: Cyclin-dependent kinase 5 activator 1 (CDK5R1)

Cyclin-dependent kinase 5 activator 1 (CDK5R1) is a 307-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q15078.

Gene
CDK5R1
Organism
Homo sapiens
Length
307 residues
Mean pLDDT
72.9
Model
AF-Q15078-F1 v6
Model created
1 Aug 2025
PDB structures
11

Explore in 3D Color by confidence AlphaFold DB UniProt

Model confidence (pLDDT)

The mean pLDDT of this model is 72.9 (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 accurate48%
70 to 90Confident: backbone generally right3%
50 to 70Low: treat with caution19%
Below 50Very low: often disordered regions31%

What pLDDT means and how to read it

Function

p35 is a neuron specific activator of CDK5. The complex p35/CDK5 is required for neurite outgrowth and cortical lamination. Involved in dendritic spine morphogenesis by mediating the EFNA1-EPHA4 signaling. Activator of TPKII. The complex p35/CDK5 participates in the regulation of the circadian clock by modulating the function of CLOCK protein: phosphorylates CLOCK at 'Thr-451' and 'Thr-461' and regulates the transcriptional activity of the CLOCK-BMAL1 heterodimer in association with altered stability and subcellular distribution

Subunit structure

Heterodimer composed of a catalytic subunit CDK5 and a regulatory subunit CDK5R1 (p25) and macromolecular complex composed of at least CDK5, CDK5R1 (p35) and CDK5RAP1 or CDK5RAP2 or CDK5RAP3 (PubMed:15689152, PubMed:16039528, PubMed:17671990). Only the heterodimer shows kinase activity (PubMed:15689152, PubMed:16039528, PubMed:17671990). Interacts with EPHA4 and NGEF; may mediate the activation…

Subcellular location

Cell membrane, Cell projection, neuron projection, Nucleus, Cytoplasm, perinuclear region, Perikaryon

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
3O0GX-ray1.95 ÅD/E=145-293
7VDPX-ray2.09 ÅC/D=100-307
1UNLX-ray2.2 ÅD/E=100-307
1UNGX-ray2.3 ÅD/E=100-307
1UNHX-ray2.35 ÅD/E=100-307
6LDPX-ray2.35 ÅA/B=298-307
7VDRX-ray2.55 ÅC/D=100-307
1H4LX-ray2.65 ÅD/E=147-293
7VDQX-ray2.91 ÅC/D=100-307
7VDSX-ray3.05 ÅC/D=100-307
7CNGX-ray3.49 ÅA/B=298-307

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.