P11802: Cyclin-dependent kinase 4 (CDK4)

Cyclin-dependent kinase 4 (CDK4) is a 303-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P11802.

Gene
CDK4
Organism
Homo sapiens
Length
303 residues
Mean pLDDT
86.8
Model
AF-P11802-F1 v6
Model created
1 Aug 2025
PDB structures
15

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Model confidence (pLDDT)

The mean pLDDT of this model is 86.8 (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 accurate67%
70 to 90Confident: backbone generally right19%
50 to 70Low: treat with caution8%
Below 50Very low: often disordered regions7%

What pLDDT means and how to read it

Function

Ser/Thr-kinase component of cyclin D-CDK4 (DC) complexes that phosphorylate and inhibit members of the retinoblastoma (RB) protein family including RB1 and regulate the cell-cycle during G(1)/S transition. Phosphorylation of RB1 allows dissociation of the transcription factor E2F from the RB/E2F complexes and the subsequent transcription of E2F target genes which are responsible for the progression through the G(1) phase. Hypophosphorylates RB1 in early G(1) phase. Cyclin D-CDK4 complexes are major integrators of various mitogenenic and antimitogenic signals. Also phosphorylates SMAD3 in a cell-cycle-dependent manner and represses its transcriptional activity. Component of the ternary…

Subunit structure

Component of the D-CDK4 complex, composed of CDK4 and some D-type G1 cyclin (CCND1, CCND2 or CCND3). Interacts directly in the complex with CCND1, CCND2 or CCND3. Interacts with SEI1 and ZNF655. Forms a ternary complex, cyclin D-CDK4-CDKN1B, involved in modulating CDK4 enzymatic activity. Interacts directly with CDKN1B (phosphorylated on 'Tyr-88' and 'Tyr-89'); the interaction allows assembly of…

Subcellular location

Cytoplasm, Nucleus, 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 ÅB/D=1-303
2W96X-ray2.3 ÅB=1-303
6P8EX-ray2.3 ÅB=2-303
2W9ZX-ray2.45 ÅB=1-303
7SJ3X-ray2.51 ÅA=2-303
2W99X-ray2.8 ÅB=1-303
6P8GX-ray2.8 ÅB=2-303
2W9FX-ray2.85 ÅB=1-303
6P8FX-ray2.89 ÅB=2-303
3G33X-ray3.0 ÅA/C=1-303
6P8HX-ray3.19 ÅB=2-303
5FWKEM3.9 ÅK=1-303
5FWPEM7.2 ÅK=1-303
5FWMEM8.0 ÅK=1-303
5FWLEM9.0 ÅK=1-303

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