O00187: Mannan-binding lectin serine protease 2 (MASP2)

Mannan-binding lectin serine protease 2 (MASP2) is a 686-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O00187.

Gene
MASP2
Organism
Homo sapiens
Length
686 residues
Mean pLDDT
89.4
Model
AF-O00187-F1 v6
Model created
1 Aug 2025
PDB structures
10

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Model confidence (pLDDT)

The mean pLDDT of this model is 89.4 (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 accurate73%
70 to 90Confident: backbone generally right21%
50 to 70Low: treat with caution2%
Below 50Very low: often disordered regions4%

What pLDDT means and how to read it

Function

Precursor of a serum protease that activates the lectin 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:11527969, PubMed:22691502). The lectin complement system is activated following association of lectins, such as MBL2, FCN1, FCN2 or FCN3, to carbohydrates on the pathogen surface (PubMed:22691502, PubMed:22966085). MASP2 is cleaved and activated by MASP1 in response to lectin-binding to pathogen carbohydrates (PubMed:10946292, PubMed:22949645, PubMed:22966085, PubMed:9087411). Can activate prothrombin to thrombin (PubMed:39924859)

Subunit structure

Homodimer; disulfide-linked (PubMed:15117939, PubMed:15364579). Interacts with MBL2 and FCN2; requires calcium ions (PubMed:15117939). Interacts with SERPING1 (PubMed:10946292). Interacts with guianensin, an anticoagulant and anti-complement protein from Simulium guianense saliva; the interaction results in the inhibition of MASP2 enzymatic activity (PubMed:39924859)

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
3TVJX-ray1.28 ÅA=363-444, B=445-686
9D40X-ray1.76 ÅA=363-686
9D17X-ray1.97 ÅA=363-686
9D3YX-ray2.08 ÅA=363-686
1ZJKX-ray2.18 ÅA=287-686
1Q3XX-ray2.23 ÅA/B=363-686
9D4DX-ray2.36 ÅA=363-686
7PQNX-ray2.4 ÅA/aa=363-444, B/bb=445-686
1SZBX-ray2.5 ÅA/B=16-181
5JPMX-ray3.75 ÅG/I=291-444, H/J=445-686

More AlphaFold highlights

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