P42768: Actin nucleation-promoting factor WAS (WAS)

Actin nucleation-promoting factor WAS (WAS) is a 502-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P42768.

Gene
WAS
Organism
Homo sapiens
Length
502 residues
Mean pLDDT
69.4
Model
AF-P42768-F1 v6
Model created
1 Aug 2025
PDB structures
6

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Model confidence (pLDDT)

The mean pLDDT of this model is 69.4 (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 accurate24%
70 to 90Confident: backbone generally right27%
50 to 70Low: treat with caution26%
Below 50Very low: often disordered regions24%

What pLDDT means and how to read it

Function

Effector protein for Rho-type GTPases that regulates actin filament reorganization via its interaction with the Arp2/3 complex (PubMed:12235133, PubMed:12769847, PubMed:16275905). Important for efficient actin polymerization (PubMed:12235133, PubMed:16275905, PubMed:8625410). Possible regulator of lymphocyte and platelet function (PubMed:9405671). Mediates actin filament reorganization and the formation of actin pedestals upon infection by pathogenic bacteria (PubMed:18650809). In addition to its role in the cytoplasmic cytoskeleton, also promotes actin polymerization in the nucleus, thereby regulating gene transcription and repair of damaged DNA (PubMed:20574068). Promotes homologous…

Subunit structure

Binds the Arp2/3 complex (PubMed:12769847). Interacts with CDC42, RAC, NCK, HCK, FYN, SRC kinase FGR, BTK, ABL1, PSTPIP1, WIP, and to the p85 subunit of PLC-gamma (PubMed:10360578, PubMed:12235133, PubMed:15235593, PubMed:8643625, PubMed:9405671, PubMed:16246732). Interacts (via C-terminus) with ALDOA (PubMed:17329259). Interacts with NCK1 (via SH3 domains) (By similarity). Interacts with FCHSD2…

Subcellular location

Cytoplasm, cytoskeleton, Nucleus

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
2OT0X-ray2.05 ÅE/F/G/H=488-502
2A3ZX-ray2.08 ÅC=430-458
1CEENMRB=230-288
1EJ5NMRA=242-310
1T84NMRA=242-310
2K42NMRA=242-310

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