P61965: WD repeat-containing protein 5 (Wdr5)

WD repeat-containing protein 5 (Wdr5) is a 334-residue protein from Mus musculus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P61965.

Gene
Wdr5
Organism
Mus musculus
Length
334 residues
Mean pLDDT
93.5
Model
AF-P61965-F1 v6
Model created
1 Aug 2025
PDB structures
5

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Model confidence (pLDDT)

The mean pLDDT of this model is 93.5 (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 accurate90%
70 to 90Confident: backbone generally right2%
50 to 70Low: treat with caution2%
Below 50Very low: often disordered regions7%

What pLDDT means and how to read it

Function

Contributes to histone modification (By similarity). May position the N-terminus of histone H3 for efficient trimethylation at 'Lys-4' (By similarity). As part of the MLL1/MLL complex it is involved in methylation and dimethylation at 'Lys-4' of histone H3 (By similarity). H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation (By similarity). As part of the NSL complex it may be involved in acetylation of nucleosomal histone H4 on several lysine residues (By similarity). May regulate osteoblasts differentiation (PubMed:11551928). In association with RBBP5 and ASH2L, stimulates the histone methyltransferase activities of KMT2A, KMT2B, KMT2C, KMT2D,…

Subunit structure

Interacts with PAXBP1; the interaction is direct and links a WDR5-containing histone methyltransferase complex to PAX7 and PAX3 (PubMed:22862948). Interacts with HCFC1 (By similarity). Component of the ATAC complex, a complex with histone acetyltransferase activity on histones H3 and H4 (By similarity). Component of the SET1 complex, at least composed of the catalytic subunit (SETD1A or SETD1B),…

Subcellular location

Nucleus

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
8OK1X-ray1.38 ÅA=32-334
8OKFX-ray1.85 ÅA=22-334
2XL2X-ray2.4 ÅA/B=1-334
8YDDX-ray2.5 ÅA/B/C=22-334
2XL3X-ray2.7 ÅA/B=1-334

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