Q00987: E3 ubiquitin-protein ligase Mdm2 (MDM2)

E3 ubiquitin-protein ligase Mdm2 (MDM2) is a 491-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q00987.

Gene
MDM2
Organism
Homo sapiens
Length
491 residues
Mean pLDDT
62.6
Model
AF-Q00987-F1 v6
Model created
1 Aug 2025
PDB structures
147

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Model confidence (pLDDT)

The mean pLDDT of this model is 62.6 (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 right9%
50 to 70Low: treat with caution14%
Below 50Very low: often disordered regions48%

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 (PubMed:29681526, PubMed:21317885). 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…

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 (PubMed:36897777). Although FAM193A interacts with MDM4 and MDM2, it does not affect formation of the p53-MDM2-MDM4 transcriptional repressor complex…

Subcellular location

Nucleus, nucleoplasm, Cytoplasm, Nucleus, nucleolus, Nucleus

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
6Q9LX-ray1.13 ÅA/B=17-111
5C5AX-ray1.15 ÅA/B=20-111
6Q9OX-ray1.21 ÅA/B=17-111
5ZXFX-ray1.25 ÅA=24-110
7QDQX-ray1.26 ÅA=20-111
8F10X-ray1.28 ÅA=17-111
8P0DX-ray1.31 ÅB=161-191
5Z02X-ray1.35 ÅA=24-112
8J81X-ray1.35 ÅA=17-111
4OGNX-ray1.38 ÅA=6-110
2AXIX-ray1.4 ÅA=17-125
7KJMX-ray1.4 ÅA/C=25-109
8F13X-ray1.4 ÅA=17-111
6SQOX-ray1.41 ÅA/D=430-491
4WT2X-ray1.42 ÅA=6-110
4UE1X-ray1.45 ÅA/B/C/D=17-125
7NUSX-ray1.45 ÅA/B/C=17-111
8PWCX-ray1.46 ÅA/B/C=17-125
8GCGX-ray1.47 ÅA=17-125
4OGTX-ray1.54 ÅA=6-110

Showing 20 of 147 experimental structures (best resolution first).

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