O96013: Serine/threonine-protein kinase PAK 4 (PAK4)

Serine/threonine-protein kinase PAK 4 (PAK4) is a 591-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O96013.

Gene
PAK4
Organism
Homo sapiens
Length
591 residues
Mean pLDDT
70.1
Model
AF-O96013-F1 v6
Model created
1 Aug 2025
PDB structures
49

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Model confidence (pLDDT)

The mean pLDDT of this model is 70.1 (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 accurate44%
70 to 90Confident: backbone generally right11%
50 to 70Low: treat with caution7%
Below 50Very low: often disordered regions38%

What pLDDT means and how to read it

Function

Serine/threonine-protein kinase that plays a role in a variety of different signaling pathways including cytoskeleton regulation, cell adhesion turnover, cell migration, growth, proliferation or cell survival (PubMed:26598620). Activation by various effectors including growth factor receptors or active CDC42 and RAC1 results in a conformational change and a subsequent autophosphorylation on several serine and/or threonine residues. Phosphorylates and inactivates the protein phosphatase SSH1, leading to increased inhibitory phosphorylation of the actin binding/depolymerizing factor cofilin. Decreased cofilin activity may lead to stabilization of actin filaments. Phosphorylates LIMK1, a…

Subunit structure

Interacts with FGFR2 and GRB2 (By similarity). Interacts tightly with GTP-bound but not GDP-bound CDC42/p21 and weakly with RAC1 (PubMed:15827085, PubMed:26598620). Interacts with INKA1 (PubMed:26607847). Interacts with SH3RF2 (PubMed:24130170). Interacts with RHOU and PAXI; the PAK4-RHOU complex protects RHOU from ubiquitination and acts as a scaffold to support paxillin/PAXI phosphorylation…

Subcellular location

Cytoplasm

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
2J0IX-ray1.6 ÅA=291-591
2Q0NX-ray1.75 ÅA=291-591
5VEFX-ray1.75 ÅA=286-591
5ZJWX-ray1.8 ÅA=300-591
4JDIX-ray1.85 ÅA=286-591
5XVAX-ray1.85 ÅA=300-591
8AHGX-ray1.89 ÅA=300-591
6WLYX-ray1.9 ÅA=286-591
7S48X-ray1.9 ÅA=286-591
4FIHX-ray1.97 ÅA=286-591
4FIIX-ray2.0 ÅA=286-591, B=49-56
4JDHX-ray2.0 ÅA=286-591
7S47X-ray2.0 ÅA=286-591
8AHHX-ray2.04 ÅA=300-591
4XBUX-ray2.06 ÅA=286-591
2OV2X-ray2.1 ÅI/J/K/L/M/N/O/P=10-44
2X4ZX-ray2.1 ÅA=296-591
5XVGX-ray2.1 ÅA=300-591
7S46X-ray2.1 ÅA=286-591
4APPX-ray2.2 ÅA=300-591

Showing 20 of 49 experimental structures (best resolution first).

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