P26358: DNA (cytosine-5)-methyltransferase 1 (DNMT1)

DNA (cytosine-5)-methyltransferase 1 (DNMT1) is a 1616-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P26358.

Gene
DNMT1
Organism
Homo sapiens
Length
1616 residues
Mean pLDDT
77.8
Model
AF-P26358-F1 v6
Model created
1 Aug 2025
PDB structures
27

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Model confidence (pLDDT)

The mean pLDDT of this model is 77.8 (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 accurate46%
70 to 90Confident: backbone generally right28%
50 to 70Low: treat with caution5%
Below 50Very low: often disordered regions21%

What pLDDT means and how to read it

Function

DNA methyltransferase that methylates CpG residues (PubMed:17200670, PubMed:18754681, PubMed:21745816, PubMed:26070743). Preferentially methylates hemimethylated DNA (PubMed:21745816, PubMed:26070743). Associates with DNA replication sites in S phase maintaining the methylation pattern in the newly synthesized strand, that is essential for epigenetic inheritance (PubMed:17200670, PubMed:21745816). Associates with chromatin during G2 and M phases to maintain DNA methylation independently of replication (PubMed:21745816). It is responsible for maintaining methylation patterns established in development (PubMed:21745816). DNA methylation is coordinated with methylation of histones…

Subunit structure

Homodimer (PubMed:19173286). Forms a stable complex with E2F1, BB1 and HDAC1 (PubMed:10888886). Forms a complex with DMAP1 and HDAC2, with direct interaction (PubMed:10888872). Interacts with the PRC2/EED-EZH2 complex (PubMed:16357870). Probably part of a corepressor complex containing ZNF304, TRIM28, SETDB1 and DNMT1 (PubMed:24623306). Interacts with UHRF1; promoting its recruitment to…

Subcellular location

Nucleus, Chromosome

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
6X9JX-ray1.79 ÅA=729-1600
6L1FX-ray1.9 ÅA=140-145
7SFCX-ray1.97 ÅA=729-1600
5WVOX-ray2.0 ÅC=351-600
5YDRX-ray2.0 ÅB=351-599
7SFFX-ray2.05 ÅA=729-1600
7SFDX-ray2.09 ÅA=729-1600
6X9IX-ray2.2 ÅA=729-1600
7XIBEM2.23 ÅA=351-1616
6K3AX-ray2.3 ÅB/D/F=161-180
3EPZX-ray2.31 ÅA/B=351-600
7SFGX-ray2.43 ÅA=729-1600
3SWRX-ray2.49 ÅA=601-1600
7XI9EM2.52 ÅA=351-1616
7SFEX-ray2.55 ÅA=729-1600
4WXXX-ray2.62 ÅA/B=351-1600
6X9KX-ray2.65 ÅA=729-1600
9V36EM2.77 ÅA=698-1616
4Z96X-ray2.85 ÅC=1097-1129
9V5PEM2.85 ÅA=698-1616

Showing 20 of 27 experimental structures (best resolution first).

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