Q8NHY2: E3 ubiquitin-protein ligase COP1 (COP1)

E3 ubiquitin-protein ligase COP1 (COP1) is a 731-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q8NHY2.

Gene
COP1
Organism
Homo sapiens
Length
731 residues
Mean pLDDT
73.9
Model
AF-Q8NHY2-F1 v6
Model created
1 Aug 2025
PDB structures
7

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Model confidence (pLDDT)

The mean pLDDT of this model is 73.9 (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 accurate42%
70 to 90Confident: backbone generally right23%
50 to 70Low: treat with caution9%
Below 50Very low: often disordered regions26%

What pLDDT means and how to read it

Function

E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Involved in JUN ubiquitination and degradation. Directly involved in p53 (TP53) ubiquitination and degradation, thereby abolishing p53-dependent transcription and apoptosis. Ubiquitinates p53 independently of MDM2 or RCHY1. Probably mediates E3 ubiquitin ligase activity by functioning as the essential RING domain subunit of larger E3 complexes. In contrast, it does not constitute the catalytic RING subunit…

Subunit structure

Homodimer. Homodimerization is mediated by the coiled coil domain. Component of the DCX DET1-COP1 ubiquitin ligase complex at least composed of RBX1, DET1, DDB1, CUL4A and COP1. Isoform 2 does not interact with CUL4A but still binds to RBX1, suggesting that the interaction may be mediated by another cullin protein. Isoform 1 and isoform 2 interact with CUL5 but not with CUL1, CUL2 not CUL3.…

Subcellular location

Nucleus speckle, Cytoplasm

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
5HQGX-ray2.0 ÅA=376-731
9LTREM3.03 ÅA/C=1-731
9LU1EM3.62 ÅA/E=1-731
9W90EM3.7 ÅA/C=1-731
5IGQX-ray3.9 ÅA/B/C/D/E/F=386-731
9M0YEM4.25 ÅA/B/C/D/E/F/G/J=1-731
9LULEM4.99 ÅH/I/K/M/N/O/W/X=128-731

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