P53165: SAGA complex subunit SGF73 (SGF73)

SAGA complex subunit SGF73 (SGF73) is a 657-residue protein from Saccharomyces cerevisiae (strain ATCC 204508 / S288c). This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P53165.

Gene
SGF73
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Length
657 residues
Mean pLDDT
64.0
Model
AF-P53165-F1 v6
Model created
1 Aug 2025
PDB structures
14

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Model confidence (pLDDT)

The mean pLDDT of this model is 64.0 (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 accurate18%
70 to 90Confident: backbone generally right28%
50 to 70Low: treat with caution13%
Below 50Very low: often disordered regions41%

What pLDDT means and how to read it

Function

Component of the transcription coactivator SAGA complex. SAGA acts as a general cofactor required for essentially all RNA polymerase II transcription (PubMed:25216679). At the promoters, SAGA is required for transcription pre-initiation complex (PIC) recruitment. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction (via core/TAF module) and promoter selectivity, interaction with transcription activators (via Tra1/SPT module), and chromatin modification through histone acetylation (via HAT module) and deubiquitination (via DUB module) (PubMed:17090597, PubMed:31969703). SAGA preferentially acetylates histones H3 (to form H3K9ac,…

Subunit structure

Component of the 1.8 MDa SAGA (Spt-Ada-Gcn5 acetyltransferase) complex, which is composed of 19 subunits TRA1, SPT7, TAF5, NGG1/ADA3, SGF73, SPT20/ADA5, SPT8, TAF12, TAF6, HFI1/ADA1, UBP8, GCN5, ADA2, SPT3, SGF29, TAF10, TAF9, SGF11 and SUS1 (PubMed:12052880, PubMed:17090597, PubMed:31969703). The SAGA complex is composed of 4 modules, namely the HAT (histone acetyltransferase) module (GCN5,…

Subcellular location

Nucleus, Cytoplasm

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
3MHSX-ray1.89 ÅE=1-96
4FK5X-ray2.03 ÅE=1-96
6AQRX-ray2.1 ÅE=1-96
4WA6X-ray2.36 ÅE/H=1-96
3MHHX-ray2.45 ÅE=1-96
4FIPX-ray2.69 ÅD/H=1-96
3M99X-ray2.7 ÅD=1-104
4W4UX-ray2.8 ÅE/H=1-96
4FJCX-ray2.83 ÅD/H=1-96
6T9KEM3.3 ÅQ=1-657
6T9LEM3.6 ÅN=1-657
4ZUXX-ray3.82 ÅY/d/i/n=1-104
6T9IEM3.9 ÅQ=1-657
2LO3NMRA=59-102

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