P02748: Complement component C9 (C9)

Complement component C9 (C9) is a 559-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P02748.

Gene
C9
Organism
Homo sapiens
Length
559 residues
Mean pLDDT
78.8
Model
AF-P02748-F1 v6
Model created
1 Aug 2025
PDB structures
9

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Model confidence (pLDDT)

The mean pLDDT of this model is 78.8 (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 accurate39%
70 to 90Confident: backbone generally right39%
50 to 70Low: treat with caution7%
Below 50Very low: often disordered regions16%

What pLDDT means and how to read it

Function

Pore-forming component of the membrane attack complex (MAC), a multiprotein complex activated by the complement cascade, which inserts into a target cell membrane and forms a pore, leading to target cell membrane rupture and cell lysis (PubMed:22832194, PubMed:26841837, PubMed:26841934, PubMed:27052168, PubMed:30552328, PubMed:6177822, PubMed:9212048, PubMed:9634479). The MAC is initiated by proteolytic cleavage of C5 into complement C5b in response to the classical, alternative, lectin and GZMK complement pathways (PubMed:39914456, PubMed:39814882, PubMed:9212048, PubMed:9634479). The complement pathways consist in a cascade of proteins that leads to phagocytosis and breakdown of…

Subunit structure

Homooligomer; about 20 C9 chains oligomerize to give rise to a huge beta-barrel that forms a 100 Angstrom diameter pore in target membranes (PubMed:26841934, PubMed:30111885, PubMed:34752492). Component of the membrane attack complex (MAC), composed of complement C5b, C6, C7, C8A, C8B, C8G and multiple copies of the pore-forming subunit C9 (PubMed:22832194, PubMed:26841837, PubMed:26841934,…

Subcellular location

Secreted, Target cell membrane

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
8DE6EM3.2 ÅA/C/G=21-559
7NYDEM3.3 ÅG/H=22-559
8B0GEM3.3 ÅH/I/J=1-559
8B0HEM3.3 ÅH/I=1-559
7NYCEM3.5 ÅG/H/I=22-559
6DLWEM3.9 ÅA/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V=22-559
6H03EM5.6 ÅG/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=22-559
6H04EM5.6 ÅG/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=22-559
5FMWEM6.7 ÅA/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V=39-544

More AlphaFold highlights

About this viewer

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