Q15393: Splicing factor 3B subunit 3 (SF3B3)

Splicing factor 3B subunit 3 (SF3B3) is a 1217-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q15393.

Gene
SF3B3
Organism
Homo sapiens
Length
1217 residues
Mean pLDDT
92.3
Model
AF-Q15393-F1 v6
Model created
1 Aug 2025
PDB structures
64

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Model confidence (pLDDT)

The mean pLDDT of this model is 92.3 (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 bandMeaningShare of residues
Above 90Very high: backbone and side chains are usually accurate79%
70 to 90Confident: backbone generally right19%
50 to 70Low: treat with caution2%
Below 50Very low: often disordered regions1%

What pLDDT means and how to read it

Function

Component of the 17S U2 SnRNP complex of the spliceosome, a large ribonucleoprotein complex that removes introns from transcribed pre-mRNAs (PubMed:10490618, PubMed:10882114, PubMed:12234937, PubMed:27720643, PubMed:28781166, PubMed:32494006, PubMed:34822310). The 17S U2 SnRNP complex (1) directly participates in early spliceosome assembly and (2) mediates recognition of the intron branch site during pre-mRNA splicing by promoting the selection of the pre-mRNA branch-site adenosine, the nucleophile for the first step of splicing (PubMed:12234937, PubMed:32494006, PubMed:34822310). Within the 17S U2 SnRNP complex, SF3B3 is part of the SF3B subcomplex, which is required for 'A' complex…

Subunit structure

Component of the 17S U2 SnRNP complex, a ribonucleoprotein complex that contains small nuclear RNA (snRNA) U2 and a number of specific proteins (PubMed:11991638, PubMed:12234937, PubMed:15146077, PubMed:32494006, PubMed:34822310, PubMed:36797247). Part of the SF3B subcomplex of the 17S U2 SnRNP complex (PubMed:12234937, PubMed:12738865, PubMed:27720643, PubMed:28541300). SF3B associates with the…

Subcellular location

Nucleus

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
7Q4OEM2.2 ÅC=1-1217
7Q4PEM2.2 ÅC=1-1217
7Q3LEM2.3 ÅC=1-1217
7B9CX-ray2.4 ÅA=916-1216
9RDKEM2.41 ÅA=1-1217
7EVOEM2.5 Å3=1-1217
7EVNEM2.6 ÅA=1-1217
8H6LEM2.6 Å2I=1-1217
8H6KEM2.7 Å2I=1-1217
8HK1EM2.7 Å3=1-1217
7DVQEM2.89 Å3=1-1217
7B0IX-ray3.0 ÅA=1-442, A=768-1217
7B91X-ray3.0 ÅA=1-442, A=768-1216
7B92X-ray3.0 ÅA=1-442, A=768-1216
7OMFX-ray3.0 ÅA=1-442, A=768-1217
7VPXEM3.0 Å3=1-1217
8I0REM3.0 Å3=1-1217
8I0TEM3.0 Å3=1-1217
8I0VEM3.0 Å3=1-1217
6EN4X-ray3.08 ÅA=1-1217

Showing 20 of 64 experimental structures (best resolution first).

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