P24279: DNA replication licensing factor MCM3 (MCM3)

DNA replication licensing factor MCM3 (MCM3) is a 971-residue protein from Saccharomyces cerevisiae (strain ATCC 204508 / S288c). This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P24279.

Gene
MCM3
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Length
971 residues
Mean pLDDT
70.8
Model
AF-P24279-F1 v6
Model created
1 Aug 2025
PDB structures
56

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Model confidence (pLDDT)

The mean pLDDT of this model is 70.8 (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 accurate10%
70 to 90Confident: backbone generally right54%
50 to 70Low: treat with caution15%
Below 50Very low: often disordered regions22%

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. Necessary for…

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. Interacts with CSM1

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 Å3/C=1-971
8RIFEM2.79 Å3/B=1-971
7V3VEM2.9 Å3/C=1-971
7P30EM3.0 Å3/B=1-971
8KG6EM3.07 Å3=1-971
7PMKEM3.2 Å3=1-971
7PMNEM3.2 Å3=1-971
7PT6EM3.2 Å3/C=1-971
7V3UEM3.2 Å3/C=1-971
9E2YEM3.2 Å3=1-971
7P5ZEM3.3 Å3/B=1-971
7QHSEM3.3 Å3=1-971
9E2WEM3.3 Å3=1-971
9GJWEM3.3 Å3=1-971
6SKOEM3.4 Å3=1-971
7Z13EM3.4 Å3/b=1-971
9GJPEM3.4 Å3=1-971
8RIGEM3.41 Å3=1-971
8B9AEM3.5 Å3=1-971
8B9BEM3.5 Å3=1-971

Showing 20 of 56 experimental structures (best resolution first).

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