WD repeat-containing protein 5 (WDR5) is a 334-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P61964.
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The mean pLDDT of this model is 93.3 (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 band | Meaning | Share of residues |
|---|---|---|
| Above 90 | Very high: backbone and side chains are usually accurate | 89% |
| 70 to 90 | Confident: backbone generally right | 2% |
| 50 to 70 | Low: treat with caution | 2% |
| Below 50 | Very low: often disordered regions | 8% |
What pLDDT means and how to read it
Contributes to histone modification (PubMed:16600877, PubMed:16829960, PubMed:19103755, PubMed:19131338, PubMed:19556245, PubMed:20018852). May position the N-terminus of histone H3 for efficient trimethylation at 'Lys-4' (PubMed:16829960). As part of the MLL1/MLL complex it is involved in methylation and dimethylation at 'Lys-4' of histone H3 (PubMed:19556245). H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation (PubMed:18840606). As part of the NSL complex it may be involved in acetylation of nucleosomal histone H4 on several lysine residues (PubMed:19103755, PubMed:20018852). May regulate osteoblasts differentiation (By similarity). In association…
Interacts with PAXBP1; the interaction is direct and links a WDR5-containing histone methyltransferase complex to PAX7 and PAX3 (By similarity). Interacts with HCFC1 (PubMed:12670868). Component of the ATAC complex, a complex with histone acetyltransferase activity on histones H3 and H4 (PubMed:19103755). Component of the SET1 complex, at least composed of the catalytic subunit (SETD1A or…
Nucleus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 6E1Z | X-ray | 1.1 Å | A/B=22-334 |
| 6U6W | X-ray | 1.2 Å | A/B=24-334 |
| 6E1Y | X-ray | 1.22 Å | A/B=22-334 |
| 6U8B | X-ray | 1.26 Å | A/B=24-334 |
| 6UHY | X-ray | 1.26 Å | A/B=31-334 |
| 6UHZ | X-ray | 1.26 Å | A/B=31-334 |
| 7BED | X-ray | 1.26 Å | A/B=1-334 |
| 24XP | X-ray | 1.3 Å | A/B=24-334 |
| 4ERY | X-ray | 1.3 Å | A=23-334 |
| 8G3E | X-ray | 1.33 Å | A/B=22-334 |
| 3EMH | X-ray | 1.37 Å | A=25-334 |
| 3UVK | X-ray | 1.4 Å | A=21-334 |
| 7WVK | X-ray | 1.42 Å | A=22-334 |
| 2H14 | X-ray | 1.48 Å | A=22-334 |
| 9UXM | X-ray | 1.48 Å | A=24-334 |
| 6UJH | X-ray | 1.49 Å | A/B=22-334 |
| 2H6N | X-ray | 1.5 Å | A/B=23-334 |
| 4CY1 | X-ray | 1.5 Å | A/B=23-334 |
| 4EWR | X-ray | 1.5 Å | A=23-334 |
| 4QL1 | X-ray | 1.5 Å | A/B=24-334 |
Showing 20 of 192 experimental structures (best resolution first).
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