Q641Q2: WASH complex subunit 2A (WASHC2A)

WASH complex subunit 2A (WASHC2A) is a 1341-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q641Q2.

Gene
WASHC2A
Organism
Homo sapiens
Length
1341 residues
Mean pLDDT
47.8
Model
AF-Q641Q2-F1 v6
Model created
1 Aug 2025
PDB structures
7

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Model confidence (pLDDT)

The mean pLDDT of this model is 47.8 (very 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 accurate4%
70 to 90Confident: backbone generally right10%
50 to 70Low: treat with caution15%
Below 50Very low: often disordered regions72%

What pLDDT means and how to read it

Function

Acts at least in part as component of the WASH core complex whose assembly at the surface of endosomes inhibits WASH nucleation-promoting factor (NPF) activity in recruiting and activating the Arp2/3 complex to induce actin polymerization and is involved in the fission of tubules that serve as transport intermediates during endosome sorting. Mediates the recruitment of the WASH core complex to endosome membranes via binding to phospholipids and VPS35 of the retromer CSC. Mediates the recruitment of the F-actin-capping protein dimer to the WASH core complex probably promoting localized F-actin polymerization needed for vesicle scission. Via its C-terminus binds various phospholipids, most…

Subunit structure

Component of the WASH core complex also described as WASH regulatory complex (SHRC) composed of WASH (WASHC1, WASH2P or WASH3P), WASHC2 (WASHC2A or WASHC2C), WASHC3, WASHC4 and WASHC5; in the complex interacts (via N-terminus) directly with WASHC1. The WASH core complex associates with the F-actin-capping protein dimer (formed by CAPZA1, CAPZA2 or CAPZA3 and CAPZB) in a transient or…

Subcellular location

Early endosome membrane, Cell membrane

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
8TTVX-ray2.0 ÅB=1289-1302
8TTDX-ray2.01 ÅB=1328-1341
8TTTX-ray2.35 ÅB=1124-1140
8TTUX-ray2.36 ÅB=1261-1274
8TTCX-ray3.01 ÅE=1289-1302
8RKSX-ray3.1 ÅI/J/K/L=1332-1338
8TTAX-ray3.46 ÅE/F=1328-1341

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