P42568: Protein AF-9 (MLLT3)

Protein AF-9 (MLLT3) is a 568-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P42568.

Gene
MLLT3
Organism
Homo sapiens
Length
568 residues
Mean pLDDT
61.8
Model
AF-P42568-F1 v6
Model created
1 Aug 2025
PDB structures
26

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Model confidence (pLDDT)

The mean pLDDT of this model is 61.8 (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 accurate31%
70 to 90Confident: backbone generally right5%
50 to 70Low: treat with caution8%
Below 50Very low: often disordered regions56%

What pLDDT means and how to read it

Function

Chromatin reader component of the super elongation complex (SEC), a complex required to increase the catalytic rate of RNA polymerase II transcription by suppressing transient pausing by the polymerase at multiple sites along the DNA (PubMed:20159561, PubMed:20471948, PubMed:25417107, PubMed:27105114, PubMed:27545619). Specifically recognizes and binds acylated histone H3, with a preference for histone H3 that is crotonylated (PubMed:25417107, PubMed:27105114, PubMed:27545619, PubMed:30374167, PubMed:30385749). Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors (PubMed:25417107, PubMed:27105114, PubMed:27545619). Recognizes and binds…

Subunit structure

Component of the super elongation complex (SEC), at least composed of EAF1, EAF2, CDK9, MLLT3/AF9, AFF (AFF1 or AFF4), the P-TEFb complex and ELL (ELL, ELL2 or ELL3) (PubMed:20159561, PubMed:20471948, PubMed:22195968, PubMed:23260655, PubMed:25417107, PubMed:30134174). Interacts with BCOR (PubMed:10898795). Interacts with CBX8 (PubMed:11313972). Interacts with ALKBH4 (PubMed:23145062). Interacts…

Subcellular location

Nucleus, Chromosome

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
8PJ7X-ray1.26 ÅA=1-142
7VKGX-ray1.83 ÅA=1-138
5YYFX-ray1.9 ÅA/C=1-138
6MILX-ray1.93 ÅA/C=1-138
7EICX-ray1.95 ÅA/B=1-138
7EIDX-ray2.0 ÅA/B=1-138
8TLXX-ray2.1 ÅA=500-568
9ARRX-ray2.1 ÅA/B=1-138
8TLWX-ray2.11 ÅA=500-568
6LS6X-ray2.2 ÅA/B=1-138
7VKHX-ray2.25 ÅA/B=1-138
4TMPX-ray2.3 ÅA/C=1-138
9AROX-ray2.3 ÅA/B/C/D=1-138
6MIMX-ray2.52 ÅA/C=1-138
8TLVX-ray2.66 ÅA=500-568
5HJBX-ray2.7 ÅA=1-138
9IM4X-ray2.79 ÅA/B=1-138
5HJDX-ray2.81 ÅA/C/E/G/K/N/Q/T=1-138
8Z73X-ray2.91 ÅA/B/D/F=1-138
6L5ZX-ray3.05 ÅA=1-138

Showing 20 of 26 experimental structures (best resolution first).

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