Q8WWW0: Ras association domain-containing protein 5 (RASSF5)

Ras association domain-containing protein 5 (RASSF5) is a 418-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q8WWW0.

Gene
RASSF5
Organism
Homo sapiens
Length
418 residues
Mean pLDDT
67.3
Model
AF-Q8WWW0-F1 v6
Model created
1 Aug 2025
PDB structures
2

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Model confidence (pLDDT)

The mean pLDDT of this model is 67.3 (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 right35%
50 to 70Low: treat with caution9%
Below 50Very low: often disordered regions32%

What pLDDT means and how to read it

Function

Potential tumor suppressor. Seems to be involved in lymphocyte adhesion by linking RAP1A activation upon T-cell receptor or chemokine stimulation to integrin activation. Isoform 2 stimulates lymphocyte polarization and the patch-like distribution of ITGAL/LFA-1, resulting in an enhanced adhesion to ICAM1. Together with RAP1A may participate in regulation of microtubule growth. The association of isoform 2 with activated RAP1A is required for directional movement of endothelial cells during wound healing. May be involved in regulation of Ras apoptotic function. The RASSF5-STK4/MST1 complex may mediate HRAS and KRAS induced apoptosis

Subunit structure

Interacts directly with activated HRAS; a RASSF5-STK4/MST1 complex probably associates with activated HRAS (By similarity). Interacts with KRAS (By similarity). Probably interacts with Ras-like GTPases RRAS, MRAS, RAP1B, RAP2A and RALA (By similarity). Interacts with RRAS2 (PubMed:31130282). Can self-associate (By similarity). Interacts with RSSF1 isoform A (By similarity). The RSSF1 isoform…

Subcellular location

Cytoplasm, Cytoplasm, cytoskeleton

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
4OH8X-ray2.28 ÅB=366-418
4LGDX-ray3.05 ÅE/F/G/H=365-413

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