P24385: G1/S-specific cyclin-D1 (CCND1)

G1/S-specific cyclin-D1 (CCND1) is a 295-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P24385.

Gene
CCND1
Organism
Homo sapiens
Length
295 residues
Mean pLDDT
87.3
Model
AF-P24385-F1 v6
Model created
1 Aug 2025
PDB structures
11

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Model confidence (pLDDT)

The mean pLDDT of this model is 87.3 (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 right13%
50 to 70Low: treat with caution6%
Below 50Very low: often disordered regions8%

What pLDDT means and how to read it

Function

Regulatory component of the cyclin D1-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:1827756, PubMed:1833066, PubMed:19412162, PubMed:33854235, PubMed:8114739, PubMed:8302605). 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:1827756, PubMed:1833066, PubMed:19412162, PubMed:8114739, PubMed:8302605). Hypophosphorylates RB1 in early G(1) phase (PubMed:1827756, PubMed:1833066,…

Subunit structure

Interacts with either CDK4 or CDK6 protein kinase to form a serine/threonine kinase holoenzyme complex (PubMed:19237565, PubMed:8114739). The cyclin subunit imparts substrate specificity to the complex (PubMed:19237565, PubMed:20399237, PubMed:8302605, PubMed:9106657). Component of the ternary complex CCND1/CDK4/CDKN1B required for nuclear translocation and modulation of CDK4-mediated kinase…

Subcellular location

Nucleus, Cytoplasm, Nucleus membrane

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
9CSKX-ray2.25 ÅA/C=16-271
2W96X-ray2.3 ÅA=1-271
6P8EX-ray2.3 ÅA=19-267
2W9ZX-ray2.45 ÅA=16-271
5VZUX-ray2.7 ÅE/F=279-295
2W99X-ray2.8 ÅA=1-271
6P8GX-ray2.8 ÅA=19-267
2W9FX-ray2.85 ÅA=1-271
6P8FX-ray2.89 ÅA=19-267
6P8HX-ray3.19 ÅA=19-267
9IVDEM3.55 ÅE=1-295

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About this viewer

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