P53091: DNA replication licensing factor MCM6 (MCM6)

DNA replication licensing factor MCM6 (MCM6) is a 1017-residue protein from Saccharomyces cerevisiae (strain ATCC 204508 / S288c). This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P53091.

Gene
MCM6
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Length
1017 residues
Mean pLDDT
69.9
Model
AF-P53091-F1 v6
Model created
1 Aug 2025
PDB structures
55

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Model confidence (pLDDT)

The mean pLDDT of this model is 69.9 (low 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 right50%
50 to 70Low: treat with caution9%
Below 50Very low: often disordered regions27%

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…

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 MCM10

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 Å6/F=1-1017
8RIFEM2.79 Å6/E=1-1017
7V3VEM2.9 Å6/F=1-1017
7P30EM3.0 Å6/E=1-1017
8KG6EM3.07 Å6=1-1017
7PMKEM3.2 Å6=1-1017
7PMNEM3.2 Å6=1-1017
7PT6EM3.2 Å6/F=1-1017
7V3UEM3.2 Å6/F=1-1017
9E2YEM3.2 Å6=1-1017
7P5ZEM3.3 Å6/E=1-1017
7QHSEM3.3 Å6=1-1017
9E2WEM3.3 Å6=1-1017
9GJWEM3.3 Å6=1-1017
6SKOEM3.4 Å6=1-1017
7Z13EM3.4 Å6/e=1-1017
9GJPEM3.4 Å6=1-1017
8RIGEM3.41 Å6=1-1017
8B9AEM3.5 Å6=1-1017
8B9BEM3.5 Å6=1-1017

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

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