Q4Z1L3: Actin-1 (ACT1)

Actin-1 (ACT1) is a 376-residue protein from Plasmodium berghei (strain Anka). This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q4Z1L3.

Gene
ACT1
Organism
Plasmodium berghei (strain Anka)
Length
376 residues
Mean pLDDT
95.1
Model
AF-Q4Z1L3-F1 v6
Model created
1 Aug 2025
PDB structures
1

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Model confidence (pLDDT)

The mean pLDDT of this model is 95.1 (very high 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 accurate93%
70 to 90Confident: backbone generally right4%
50 to 70Low: treat with caution2%
Below 50Very low: often disordered regions1%

What pLDDT means and how to read it

Function

Actin is a highly conserved protein that polymerizes to produce filaments that form cross-linked networks in the cytoplasm (PubMed:24743229). Polymerizes into shorter and less stable actin filaments compared to ACT2/actin-2; this is thought to facilitate gliding motility and host cell invasion (PubMed:24743229). Has ATPase activity (PubMed:24743229). ATP hydrolysis leads to the formation of a stable intermediate ADP-inorganic phosphate (Pi) actin, which is followed by the release of Pi (By similarity). ATP hydrolysis affects filament stability; ADP-bound actin depolymerizes much faster than ATP- or ADP-Pi-bound actin (By similarity). Plays an essential role during the asexual blood stage…

Subunit structure

Monomer (G-actin) (PubMed:24743229). Oligomer (F-actin) (PubMed:24743229). Polymerization of globular actin (G-actin) leads to a structural filament (F-actin) in the form of a two-stranded helix (PubMed:24743229). Unlike for mammalian monomeric actin, parasite monomeric actin is able to induce oligomerization in the presence of ATP or ADP (By similarity). Mg(2+), which is used to coordinate ATP,…

Subcellular location

Cytoplasm, Nucleus, Cytoplasm, cytoskeleton

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
4CBWX-ray2.5 ÅA=5-39, A=62-376

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