Q8NHZ8: Anaphase-promoting complex subunit CDC26 (CDC26)

Anaphase-promoting complex subunit CDC26 (CDC26) is a 85-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q8NHZ8.

Gene
CDC26
Organism
Homo sapiens
Length
85 residues
Mean pLDDT
73.0
Model
AF-Q8NHZ8-F1 v6
Model created
1 Aug 2025
PDB structures
21

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Model confidence (pLDDT)

The mean pLDDT of this model is 73.0 (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 accurate34%
70 to 90Confident: backbone generally right22%
50 to 70Low: treat with caution25%
Below 50Very low: often disordered regions19%

What pLDDT means and how to read it

Function

Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through the cell cycle (PubMed:18485873, PubMed:27120157, PubMed:27509861). Together with the RING-H2 protein ANAPC11, forms the catalytic component of the E3 ubiquitin ligase complex (PubMed:18485873, PubMed:27120157, PubMed:27509861). APC/C acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains (PubMed:18485873). APC/C catalyzes assembly of branched…

Subunit structure

Component of the anaphase promoting complex/cyclosome (APC/C), composed of ANAPC1, ANAPC2, CDC27/ANAPC3, ANAPC4, ANAPC5, CDC16/ANAPC6, ANAPC7, CDC23/ANAPC8, ANAPC10, ANAPC11, CDC26/ANAPC12, ANAPC13, ANAPC15 and ANAPC16 (PubMed:25043029, PubMed:26083744, PubMed:27120157, PubMed:27509861). APC/C associates with CDC20 to form the CDC20-APC/C complex, which is crucial for metaphase/anaphase…

Subcellular location

Nucleus

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
3HYMX-ray2.8 ÅA/C/E/G/I/K=1-29
9GAWEM2.9 ÅG/W=1-85
6Q6GEM3.2 ÅG/W=1-85
6Q6HEM3.2 ÅG/W=1-85
8PKPEM3.2 ÅG/W=1-85
5G05EM3.4 ÅG/W=1-85
8TAUEM3.5 ÅG/W=1-85
4UI9EM3.6 ÅG/W=1-85
6TNTEM3.78 ÅG/W=1-85
6TLJEM3.8 ÅG/W=1-85
6TM5EM3.9 ÅG/W=1-85
9N9REM3.9 ÅG/W=1-85
9N9SEM3.9 ÅG/W=1-85
5G04EM4.0 ÅG/W=1-85
5LCWEM4.0 ÅG/W=1-85
8TAREM4.0 ÅG/W=1-85
5A31EM4.3 ÅG/W=1-85
5KHUEM4.8 ÅG/W=1-85
5KHREM6.1 ÅG/W=1-85
5L9TEM6.4 ÅG/W=1-85

Showing 20 of 21 experimental structures (best resolution first).

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