P29496: Minichromosome maintenance protein 5 (MCM5)

Minichromosome maintenance protein 5 (MCM5) is a 775-residue protein from Saccharomyces cerevisiae (strain ATCC 204508 / S288c). This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P29496.

Gene
MCM5
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Length
775 residues
Mean pLDDT
76.1
Model
AF-P29496-F1 v6
Model created
1 Aug 2025
PDB structures
53

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Model confidence (pLDDT)

The mean pLDDT of this model is 76.1 (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 accurate10%
70 to 90Confident: backbone generally right66%
50 to 70Low: treat with caution14%
Below 50Very low: often disordered regions10%

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. 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 Å5/E=1-775
8RIFEM2.79 Å5/D=1-775
7V3VEM2.9 Å5/E=1-775
7P30EM3.0 Å5/D=1-775
8KG6EM3.07 Å5=1-775
7PMKEM3.2 Å5=1-775
7PMNEM3.2 Å5=1-775
7PT6EM3.2 Å5/E=1-775
7V3UEM3.2 Å5/E=1-775
9E2YEM3.2 Å5=1-775
7P5ZEM3.3 Å5/D=1-775
9E2WEM3.3 Å5=1-775
9GJWEM3.3 Å5=1-775
6SKOEM3.4 Å5=1-775
9GJPEM3.4 Å5=1-775
8RIGEM3.41 Å5=1-775
8B9AEM3.5 Å5=1-775
8B9BEM3.5 Å5=1-775
9E2XEM3.5 Å5=1-775
3JC6EM3.7 Å5=1-775

Showing 20 of 53 experimental structures (best resolution first).

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