Q9Y4E5: E3 SUMO-protein ligase ZNF451 (ZNF451)

E3 SUMO-protein ligase ZNF451 (ZNF451) is a 1061-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9Y4E5.

Gene
ZNF451
Organism
Homo sapiens
Length
1061 residues
Mean pLDDT
68.9
Model
AF-Q9Y4E5-F1 v6
Model created
1 Aug 2025
PDB structures
1

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Model confidence (pLDDT)

The mean pLDDT of this model is 68.9 (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 accurate5%
70 to 90Confident: backbone generally right59%
50 to 70Low: treat with caution12%
Below 50Very low: often disordered regions25%

What pLDDT means and how to read it

Function

E3 SUMO-protein ligase; has a preference for SUMO2 and SUMO3 and facilitates UBE2I/UBC9-mediated sumoylation of target proteins (PubMed:26524493, PubMed:26524494). Plays a role in protein SUMO2 modification in response to stress caused by DNA damage and by proteasome inhibitors (in vitro). Required for MCM4 sumoylation (By similarity). Has no activity with SUMO1 (PubMed:26524493). Preferentially transfers an additional SUMO2 chain onto the SUMO2 consensus site 'Lys-11' (PubMed:26524493). Negatively regulates transcriptional activation mediated by the SMAD4 complex in response to TGF-beta signaling. Inhibits EP300-mediated acetylation of histone H3 at 'Lys-9' (PubMed:24324267). Plays a role…

Subunit structure

Homooligomer. Interacts (via N-terminal region) with SUMO1 (PubMed:18656483). Interacts (via N-terminal region) with SUMO2 (PubMed:18656483, PubMed:26524494). Interacts simultaneously with two SUMO2 chains (PubMed:26524493, PubMed:26524494). Identified in a complex with SUMO2 and UBE2I/UBC9, where one ZNF451 interacts with one UBE2I/UBC9 and two SUMO2 chains, one bound to the UBE2I/UBC9 active…

Subcellular location

Nucleus, Nucleus, PML body, Nucleus, nucleoplasm

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
5D2MX-ray2.4 ÅG=2-56

More AlphaFold highlights

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