P38132: DNA replication licensing factor MCM7 (MCM7)

DNA replication licensing factor MCM7 (MCM7) is a 845-residue protein from Saccharomyces cerevisiae (strain ATCC 204508 / S288c). This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P38132.

Gene
MCM7
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Length
845 residues
Mean pLDDT
77.1
Model
AF-P38132-F1 v6
Model created
1 Aug 2025
PDB structures
55

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Model confidence (pLDDT)

The mean pLDDT of this model is 77.1 (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 right65%
50 to 70Low: treat with caution13%
Below 50Very low: often disordered regions9%

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. Core component of CDC45-MCM-GINS (CMG) helicase, the molecular machine that unwinds template DNA during replication, and around which the replisome is built. 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…

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 and MCM10

Subcellular location

Cytoplasm, Nucleus

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
7W8GEM2.52 Å7/G=1-845
8RIFEM2.79 Å7/F=1-845
7V3VEM2.9 Å7/G=1-845
7P30EM3.0 Å7/F=1-845
8KG6EM3.07 Å7=1-845
7PMKEM3.2 Å7=1-845
7PMNEM3.2 Å7=1-845
7PT6EM3.2 Å7/G=1-845
7V3UEM3.2 Å7/G=1-845
9E2YEM3.2 Å7=1-845
7P5ZEM3.3 Å7/F=1-845
7QHSEM3.3 Å7=1-845
9E2WEM3.3 Å7=1-845
9GJWEM3.3 Å7=1-845
6SKOEM3.4 Å7=1-845
9GJPEM3.4 Å7=1-845
8RIGEM3.41 Å7=1-845
8B9AEM3.5 Å7=1-845
8B9BEM3.5 Å7=1-845
9E2XEM3.5 Å7=1-845

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

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