Q8IDR3: Myosin-A (MyoA)

Myosin-A (MyoA) is a 818-residue protein from Plasmodium falciparum (isolate 3D7). This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q8IDR3.

Gene
MyoA
Organism
Plasmodium falciparum (isolate 3D7)
Length
818 residues
Mean pLDDT
89.1
Model
AF-Q8IDR3-F1 v6
Model created
1 Aug 2025
PDB structures
16

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Model confidence (pLDDT)

The mean pLDDT of this model is 89.1 (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 accurate56%
70 to 90Confident: backbone generally right41%
50 to 70Low: treat with caution3%
Below 50Very low: often disordered regions0%

What pLDDT means and how to read it

Function

Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Their highly divergent tails are presumed to bind to membranous compartments, which would be moved relative to actin filaments (By similarity). In complex with light chains, binds actin and moves actin filaments (PubMed:28893907, PubMed:31337750, PubMed:33046215, PubMed:37308472). Required for parasite invasion into host red blood cells; plays a key role in host erythrocyte deformation and internalization during merozoite invasion (PubMed:31337750, PubMed:33104759)

Subunit structure

Component of the glideosome complex composed of GAP50, GAP45, GAP40, MTIP and MyoA; the complex is formed during the late schizont stage and in merozoites (PubMed:16750579, PubMed:25802338, PubMed:28893907). MyoA, MTIP and GAP45 probably form an initial complex in the cytoplasm which is then recruited to the outer face of the inner membrane complex via the interaction with GAP50…

Subcellular location

Cell membrane, Inner membrane complex

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
4MZJX-ray1.47 ÅT=799-816
4MZKX-ray1.82 ÅT=799-816
4AOMX-ray1.94 ÅT=799-816
4R1EX-ray1.98 ÅB=803-816
4MZLX-ray2.01 ÅC/D=800-816
8A12X-ray2.03 ÅA=1-818
8CDQX-ray2.21 ÅA=1-818
8CDMX-ray2.35 ÅA=1-818
6ZN3X-ray2.51 ÅC/F/I/L/O=775-816
6YCYX-ray2.55 ÅA=1-818
6I7DX-ray2.82 ÅA/B/C/D=1-768
6TU7EM3.1 ÅAP1/GP1=2-818
6YCZX-ray3.27 ÅA=1-818
6I7EX-ray3.49 ÅA=1-768
7ALNEM3.77 ÅF=1-818
6YCXX-ray3.99 ÅA/B=1-818

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