Q7YRZ8: E3 ubiquitin-protein ligase Mdm2 (MDM2)

E3 ubiquitin-protein ligase Mdm2 (MDM2) is a 491-residue protein from Felis catus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q7YRZ8.

Gene
MDM2
Organism
Felis catus
Length
491 residues
Mean pLDDT
62.9
Model
AF-Q7YRZ8-F1 v6
Model created
1 Aug 2025
PDB structures
3

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Model confidence (pLDDT)

The mean pLDDT of this model is 62.9 (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 accurate30%
70 to 90Confident: backbone generally right7%
50 to 70Low: treat with caution17%
Below 50Very low: often disordered regions46%

What pLDDT means and how to read it

Function

E3 ubiquitin-protein ligase that mediates ubiquitination of p53/TP53, leading to its degradation by the proteasome. Inhibits p53/TP53- and p73/TP73-mediated cell cycle arrest and apoptosis by binding its transcriptional activation domain. Also acts as a ubiquitin ligase E3 toward itself and ARRB1. Permits the nuclear export of p53/TP53. Promotes proteasome-dependent ubiquitin-independent degradation of retinoblastoma RB1 protein. Inhibits DAXX-mediated apoptosis by inducing its ubiquitination and degradation. Component of the TRIM28/KAP1-MDM2-p53/TP53 complex involved in stabilizing p53/TP53. Also a component of the TRIM28/KAP1-ERBB4-MDM2 complex which links growth factor and DNA damage…

Subunit structure

Component of a ternary complex composed of FAM193A, MDM4 and MDM2; interaction of FAM193A with MDM4 is mediated by the MDM4 RING-type zinc finger and results in MDM4 destabilization, leading to enhanced p53/TP53 transcriptional activity. Although FAM193A interacts with MDM4 and MDM2, it does not affect formation of the p53-MDM2-MDM4 transcriptional repressor complex. Interacts with TP53/p53 (By…

Subcellular location

Nucleus, nucleoplasm, Cytoplasm, Nucleus, nucleolus, Nucleus

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
6SQPX-ray1.21 ÅA=430-491, B/D=424-491, C=427-491
6SQSX-ray1.83 ÅA/D=428-491
6SQRX-ray2.18 ÅA=423-491, D/J=428-491, G=429-491

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