O43719: 17S U2 SnRNP complex component HTATSF1 (HTATSF1)

17S U2 SnRNP complex component HTATSF1 (HTATSF1) is a 755-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O43719.

Gene
HTATSF1
Organism
Homo sapiens
Length
755 residues
Mean pLDDT
59.1
Model
AF-O43719-F1 v6
Model created
1 Aug 2025
PDB structures
11

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Model confidence (pLDDT)

The mean pLDDT of this model is 59.1 (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 accurate17%
70 to 90Confident: backbone generally right19%
50 to 70Low: treat with caution8%
Below 50Very low: often disordered regions56%

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:30567737, 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:30567737, PubMed:32494006, PubMed:34822310). Within the 17S U2 SnRNP complex, HTATSF1 is required to stabilize the branchpoint-interacting stem loop (PubMed:34822310). HTATSF1 is displaced from the 17S U2 SnRNP 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:11780068, PubMed:30567737, PubMed:32494006, PubMed:34822310, PubMed:9710584). Within the 17S U2 SnRNP complex, interacts (via UHM region) directly with SF3B1 (PubMed:30567737). Component of a complex which is at least composed of HTATSF1/Tat-SF1,…

Subcellular location

Nucleus, Chromosome

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
6N3DX-ray1.13 ÅA=260-353
6N3EX-ray1.89 ÅA=260-353
6NSXX-ray2.0 ÅA=260-353
6N3FX-ray2.1 ÅA/C=260-353
7Q3LEM2.3 Åq=2-755
7EVOEM2.5 ÅD=1-755
8HK1EM2.7 ÅD=1-755
6Y50EM4.1 Åq=1-755
6Y53EM7.1 Åq=1-755
6Y5QEM7.1 Åq=1-755
2DITNMRA=256-354

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About this viewer

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