N1NXA6: SAGA-associated factor 11 (SGF11)

SAGA-associated factor 11 (SGF11) is a 99-residue protein from Saccharomyces cerevisiae (strain CEN.PK113-7D). This is its AlphaFold structure prediction, created 1 Jun 2022. UniProt accession: N1NXA6.

Gene
SGF11
Organism
Saccharomyces cerevisiae (strain CEN.PK113-7D)
Length
99 residues
Mean pLDDT
87.6
Model
AF-N1NXA6-F1 v6
Model created
1 Jun 2022
PDB structures
1

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Model confidence (pLDDT)

The mean pLDDT of this model is 87.6 (confident 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 accurate56%
70 to 90Confident: backbone generally right35%
50 to 70Low: treat with caution7%
Below 50Very low: often disordered regions2%

What pLDDT means and how to read it

Function

Functions as component of the transcription regulatory histone acetylation (HAT) complex SAGA. At the promoters, SAGA is required for recruitment of the basal transcription machinery. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction and promoter selectivity, interaction with transcription activators, and chromatin modification through histone acetylation and deubiquitination. SAGA acetylates nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts with DNA via upstream activating sequences (UASs). Involved in transcriptional regulation of a subset of SAGA-regulated genes. Within the…

Subunit structure

Component of the 1.8 MDa SAGA transcription coactivator-HAT complex. SAGA is built of 5 distinct domains with specialized functions. Within the SAGA complex, SUS1, SGF11, SGF73 and UBP8 form an additional subcomplex of SAGA called the DUB module (deubiquitination module). Interacts directly with SGF73, SUS1 and UBP8

Subcellular location

Nucleus

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
4W4UX-ray2.8 ÅC/G=1-99

More AlphaFold highlights

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