P29469: DNA replication licensing factor MCM2 (MCM2)

DNA replication licensing factor MCM2 (MCM2) is a 868-residue protein from Saccharomyces cerevisiae (strain ATCC 204508 / S288c). This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P29469.

Gene
MCM2
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Length
868 residues
Mean pLDDT
74.6
Model
AF-P29469-F1 v6
Model created
1 Aug 2025
PDB structures
52

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Model confidence (pLDDT)

The mean pLDDT of this model is 74.6 (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 accurate13%
70 to 90Confident: backbone generally right58%
50 to 70Low: treat with caution12%
Below 50Very low: often disordered regions17%

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; specifically the MCM2-MCM5 association is proposed to be reversible and to mediate a open ring…

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 Å2/B=1-868
8RIFEM2.79 Å2/A=1-868
7V3VEM2.9 Å2/B=1-868
7P30EM3.0 Å2/A=1-868
8KG6EM3.07 Å2=1-868
7PMKEM3.2 Å2=1-868
7PMNEM3.2 Å2=1-868
7PT6EM3.2 Å2/B=1-868
7V3UEM3.2 Å2/B=1-868
9E2YEM3.2 Å2=1-868
7P5ZEM3.3 Å2/A=1-868
9E2WEM3.3 Å2=1-868
9GJWEM3.3 Å2=1-868
6SKOEM3.4 Å2=1-868
9GJPEM3.4 Å2=1-868
8RIGEM3.41 Å2=1-868
8B9AEM3.5 Å2=1-868
8B9BEM3.5 Å2=1-868
9E2XEM3.5 Å2=1-868
3JC6EM3.7 Å2=1-868

Showing 20 of 52 experimental structures (best resolution first).

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