P10643: Complement component C7 (C7)

Complement component C7 (C7) is a 843-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P10643.

Gene
C7
Organism
Homo sapiens
Length
843 residues
Mean pLDDT
79.9
Model
AF-P10643-F1 v6
Model created
1 Aug 2025
PDB structures
8

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Model confidence (pLDDT)

The mean pLDDT of this model is 79.9 (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 accurate25%
70 to 90Confident: backbone generally right58%
50 to 70Low: treat with caution9%
Below 50Very low: often disordered regions8%

What pLDDT means and how to read it

Function

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:27052168, PubMed:30552328, PubMed:3335508). The MAC is initiated by proteolytic cleavage of C5 into complement C5b in response to the classical, alternative, lectin and GZMK complement pathways (PubMed:22832194, PubMed:30552328, PubMed:3335508, PubMed:39914456, PubMed:39814882). The complement pathways consist in a cascade of proteins that leads to phagocytosis and breakdown of pathogens and signaling that strengthens the…

Subunit structure

Monomer or dimer; as a C5b-7 complex it can also form multimeric rosettes (PubMed:22832194, PubMed:30552328). 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:27052168, PubMed:30552328, PubMed:31061395, PubMed:32569291, PubMed:3335508)

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
8B0FEM3.0 ÅC=1-843
7NYDEM3.3 ÅC=23-843
8B0GEM3.3 ÅC=1-843
8B0HEM3.3 ÅC=1-843
7NYCEM3.5 ÅC=23-843
6H03EM5.6 ÅD=23-843
6H04EM5.6 ÅD=23-843
2WCYNMRA=693-843

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