P30665: DNA replication licensing factor MCM4 (MCM4)

DNA replication licensing factor MCM4 (MCM4) is a 933-residue protein from Saccharomyces cerevisiae (strain ATCC 204508 / S288c). This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P30665.

Gene
MCM4
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Length
933 residues
Mean pLDDT
72.6
Model
AF-P30665-F1 v6
Model created
1 Aug 2025
PDB structures
55

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Model confidence (pLDDT)

The mean pLDDT of this model is 72.6 (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 accurate19%
70 to 90Confident: backbone generally right50%
50 to 70Low: treat with caution10%
Below 50Very low: often disordered regions21%

What pLDDT means and how to read it

Function

Acts as a component of the MCM2-7 complex (MCM complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity. Once loaded onto DNA, double hexamers can slide on dsDNA in the absence of ATPase activity. Required for S…

Subunit structure

Component of the MCM2-7 complex. The complex forms a toroidal hexameric ring with the proposed subunit order MCM2-MCM6-MCM4-MCM7-MCM3-MCM5; loaded onto DNA, forms a head-head double hexamer

Subcellular location

Nucleus

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
7W8GEM2.52 Å4/D=1-933
8RIFEM2.79 Å4/C=1-933
7V3VEM2.9 Å4/D=1-933
7P30EM3.0 Å4/C=1-933
8KG6EM3.07 Å4=1-933
7PMKEM3.2 Å4=1-933
7PMNEM3.2 Å4=1-933
7PT6EM3.2 Å4/D=1-933
7V3UEM3.2 Å4/D=1-933
9E2YEM3.2 Å4=1-933
7P5ZEM3.3 Å4/C=1-933
7QHSEM3.3 Å4=1-933
9E2WEM3.3 Å4=1-933
9GJWEM3.3 Å4=1-933
6SKOEM3.4 Å4=1-933
7Z13EM3.4 Å4/c=1-933
9GJPEM3.4 Å4=1-933
8RIGEM3.41 Å4=1-933
8B9AEM3.5 Å4=1-933
8B9BEM3.5 Å4=1-933

Showing 20 of 55 experimental structures (best resolution first).

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