Q9H1A4: Anaphase-promoting complex subunit 1 (ANAPC1)

Anaphase-promoting complex subunit 1 (ANAPC1) is a 1944-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9H1A4.

Gene
ANAPC1
Organism
Homo sapiens
Length
1944 residues
Mean pLDDT
77.1
Model
AF-Q9H1A4-F1 v6
Model created
1 Aug 2025
PDB structures
21

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Model confidence (pLDDT)

The mean pLDDT of this model is 77.1 (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 accurate33%
70 to 90Confident: backbone generally right42%
50 to 70Low: treat with caution9%
Below 50Very low: often disordered regions16%

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). 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 'Lys-11'-/'Lys-48'-linked branched ubiquitin chains on target proteins (PubMed:29033132). APC/C is activated by CDC20 in the metaphase/anaphase transition of the cell cycle, targeting…

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…

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
5LGGX-ray2.15 ÅA=1-33, A=70-306, A=403-613
9GAWEM2.9 ÅA=1-1944
6Q6GEM3.2 ÅA=1-306, A=397-1944
6Q6HEM3.2 ÅA=1-1944
8PKPEM3.2 ÅA=1-1944
5G05EM3.4 ÅA=1-1944
8TAUEM3.5 ÅA=1-1944
4UI9EM3.6 ÅA=1-1944
6TNTEM3.78 ÅA=1-1944
6TLJEM3.8 ÅA=1-1944
5G04EM3.9 ÅA=1-1944
6TM5EM3.9 ÅA=1-1944
9N9REM3.9 ÅA=1-1944
9N9SEM3.9 ÅA=1-1944
5LCWEM4.0 ÅA=1-1944
8TAREM4.0 ÅA=1-1944
5A31EM4.3 ÅA=11-1897
5KHUEM4.8 ÅA=1-1944
5KHREM6.1 ÅA=1-1944
5L9TEM6.4 ÅA=1-1944

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

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