P30281: G1/S-specific cyclin-D3 (CCND3)

G1/S-specific cyclin-D3 (CCND3) is a 292-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P30281.

Gene
CCND3
Organism
Homo sapiens
Length
292 residues
Mean pLDDT
86.9
Model
AF-P30281-F1 v6
Model created
1 Aug 2025
PDB structures
2

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Model confidence (pLDDT)

The mean pLDDT of this model is 86.9 (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 accurate73%
70 to 90Confident: backbone generally right11%
50 to 70Low: treat with caution3%
Below 50Very low: often disordered regions12%

What pLDDT means and how to read it

Function

Regulatory component of the cyclin D3-CDK4 (DC) complex that phosphorylates and inhibits members of the retinoblastoma (RB) protein family including RB1 and regulates the cell-cycle during G(1)/S transition (PubMed:8114739). Phosphorylation of RB1 allows dissociation of the transcription factor E2F from the RB/E2F complex and the subsequent transcription of E2F target genes which are responsible for the progression through the G(1) phase (PubMed:8114739). Hypophosphorylates RB1 in early G(1) phase (PubMed:8114739). Cyclin D-CDK4 complexes are major integrators of various mitogenenic and antimitogenic signals (PubMed:8114739). Component of the ternary complex, cyclin D3/CDK4/CDKN1B,…

Subunit structure

Interacts with the CDK4 and CDK6 protein kinases to form a serine/threonine kinase holoenzyme complex (PubMed:19237555, PubMed:8114739, PubMed:9106657). Interacts with isoform p58 of CDK11 (CDK11A or CDK11B) to form a serine/threonine kinase holoenzyme complex (PubMed:12082095). The cyclin subunit imparts substrate specificity to the complex (PubMed:8114739). Interacts with ATF5…

Subcellular location

Nucleus, Cytoplasm

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
7SJ3X-ray2.51 ÅB=1-259
3G33X-ray3.0 ÅB/D=1-292

More AlphaFold highlights

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