P07834: Cell division control protein 4 (CDC4)

Cell division control protein 4 (CDC4) is a 779-residue protein from Saccharomyces cerevisiae (strain ATCC 204508 / S288c). This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P07834.

Gene
CDC4
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Length
779 residues
Mean pLDDT
72.9
Model
AF-P07834-F1 v6
Model created
1 Aug 2025
PDB structures
4

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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 accurate58%
70 to 90Confident: backbone generally right6%
50 to 70Low: treat with caution3%
Below 50Very low: often disordered regions33%

What pLDDT means and how to read it

Function

Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Recognizes and binds to phosphorylated target proteins. Directs ubiquitination of the phosphorylated CDK inhibitor SIC1. Involved in the degradation of CDC6 together with CDC34/UBC3 and CDC53, and in restricting the degradation of FAR1 to the nucleus. Is essential for initiation of DNA replication and separation of the spindle pole bodies to form the poles of the mitotic spindle. It also plays a role in bud development, fusion of zygotic nuclei after conjugation and various aspects of sporulation.…

Subunit structure

Interacts with DCD53 and SKP1. Component of the SCF(CDC4) complex containing CDC53, SKP1, RBX1 and CDC4. CDC34. Interacts with CDC6 and CIC1. Interacts with SIC1; the interaction involves a SIC1 double phosphorylated motif (degron). Homodimerizes; the dimerization increases SIC1 ubiquitination in vitro

Subcellular location

Nucleus

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
3V7DX-ray2.31 ÅB/D=263-744
3MKSX-ray2.6 ÅB/D=263-744
2P63X-ray2.67 ÅA/B/C/D=222-273
1NEXX-ray2.7 ÅB/D=263-744

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