P09871: Complement C1s subcomponent (C1S)

Complement C1s subcomponent (C1S) is a 688-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P09871.

Gene
C1S
Organism
Homo sapiens
Length
688 residues
Mean pLDDT
87.9
Model
AF-P09871-F1 v6
Model created
1 Aug 2025
PDB structures
14

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Model confidence (pLDDT)

The mean pLDDT of this model is 87.9 (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 accurate66%
70 to 90Confident: backbone generally right25%
50 to 70Low: treat with caution6%
Below 50Very low: often disordered regions2%

What pLDDT means and how to read it

Function

Component of the complement C1 complex, a multiprotein complex that initiates the classical pathway of the complement system, a cascade of proteins that leads to phagocytosis and breakdown of pathogens and signaling that strengthens the adaptive immune system (PubMed:11445589, PubMed:16169853, PubMed:417728, PubMed:467643, PubMed:6271784, PubMed:6282646, PubMed:6319179, PubMed:70787, PubMed:9422791). C1S is activated following association of the C1 complex with immunoglobulins (IgG or IgM) complexed with antigens to form antigen-antibody complexes on the surface of pathogens (PubMed:34155115). C1S is cleaved and activated by C1R to generate C1s subcomponent heavy and light chains…

Subunit structure

Core component of the complement C1 complex, a calcium-dependent complex composed of 1 molecule of the C1Q subcomplex, 2 molecules of C1R and 2 molecules of C1S (PubMed:19473974, PubMed:2007122, PubMed:28104818, PubMed:29311313, PubMed:2988513, PubMed:2989825, PubMed:34155115, PubMed:6952210). The C1Q subcomplex is composed 18 subunits: 3 chains of C1QA, C1QB, and C1QC trimerize to form 6…

Subcellular location

Secreted, Cell surface

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
1NZIX-ray1.5 ÅA/B=16-174
1ELVX-ray1.7 ÅA=358-688
8TYPX-ray1.8 ÅA=358-688
4LOSX-ray2.0 ÅA=172-358
4LORX-ray2.5 ÅA=17-292
5UBMX-ray2.5 ÅA=437-688, B=285-436
8GMNX-ray2.6 ÅA/B/C/D=358-688
9X1HEM2.6 ÅA/B=16-292
4J1YX-ray2.66 ÅA/B=292-688
4LMFX-ray2.92 ÅA/B/C/D=17-292
4LOTX-ray2.92 ÅA=175-423
8W18X-ray3.94 ÅA=292-437, B=438-688
6F1CX-ray4.2 ÅB/D=16-292
6F1HX-ray4.5 ÅB/D=17-292

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