P0A015: Immunoglobulin G-binding protein A (spa)

Immunoglobulin G-binding protein A (spa) is a 450-residue protein from Staphylococcus aureus (strain Mu50 / ATCC 700699). This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P0A015.

Gene
spa
Organism
Staphylococcus aureus (strain Mu50 / ATCC 700699)
Length
450 residues
Mean pLDDT
68.1
Model
AF-P0A015-F1 v6
Model created
1 Aug 2025
PDB structures
5

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Model confidence (pLDDT)

The mean pLDDT of this model is 68.1 (low 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 right18%
50 to 70Low: treat with caution6%
Below 50Very low: often disordered regions37%

What pLDDT means and how to read it

Function

Plays a role in the inhibition of the host innate and adaptive immune responses. Possesses five immunoglobulin-binding domains that capture both the fragment crystallizable region (Fc region) and the Fab region (part of Ig that identifies antigen) of immunoglobulins (By similarity). In turn, Staphylococcus aureus is protected from phagocytic killing via inhibition of Ig Fc region. In addition, the host elicited B-cell response is prevented due to a decrease of antibody-secreting cell proliferation that enter the bone marrow, thereby decreasing long-term antibody production. Inhibits osteogenesis by preventing osteoblast proliferation and expression of alkaline phosphatase, type I collagen,…

Subunit structure

Interacts with host TNFRSF1A; this interaction leads to the stimulation of both surface expression and shedding of TNFRSF1A. Interacts (via B domain) with IgG1, IgG2 and IgG4; spa interferes with IgG oligomerization and IgG:C1 complement complex formation, preventing complement activation and ultimately protecting bacteria from phagocytic killing

Subcellular location

Secreted, cell wall

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
4IOIX-ray1.95 ÅH=101-151
4HJGX-ray2.0 ÅH=101-151
4HKZX-ray2.08 ÅH=101-151
8JXSEM3.0 ÅC=120-151
8JXREM3.57 ÅC=121-151

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