Q9Y5B9: FACT complex subunit SPT16 (SUPT16H)

FACT complex subunit SPT16 (SUPT16H) is a 1047-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9Y5B9.

Gene
SUPT16H
Organism
Homo sapiens
Length
1047 residues
Mean pLDDT
79.9
Model
AF-Q9Y5B9-F1 v6
Model created
1 Aug 2025
PDB structures
17

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Model confidence (pLDDT)

The mean pLDDT of this model is 79.9 (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 accurate48%
70 to 90Confident: backbone generally right31%
50 to 70Low: treat with caution7%
Below 50Very low: often disordered regions14%

What pLDDT means and how to read it

Function

Component of the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair. During transcription elongation the FACT complex acts as a histone chaperone that both destabilizes and restores nucleosomal structure. It facilitates the passage of RNA polymerase II and transcription by promoting the dissociation of one histone H2A-H2B dimer from the nucleosome, then subsequently promotes the reestablishment of the nucleosome following the passage of RNA polymerase II. The FACT complex is probably also involved in phosphorylation of…

Subunit structure

Interacts with MYOG (via C-terminal region) (By similarity). Component of the FACT complex, a stable heterodimer of SSRP1 and SUPT16H (PubMed:10421373). Also a component of a CK2-SPT16-SSRP1 complex which forms following UV irradiation, composed of SSRP1, SUPT16H, CSNK2A1, CSNK2A2 and CSNK2B (PubMed:11239457, PubMed:12393879). Interacts with NEK9 (PubMed:14660563). Binds to histone H2A-H2B…

Subcellular location

Nucleus, Chromosome

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
5E5BX-ray1.84 ÅA=2-432
5UMUX-ray1.9 ÅA/B=649-926
4Z2NX-ray1.92 ÅA=644-930
8I17X-ray1.98 ÅC/F/I=926-965
5UMTX-ray2.09 ÅA=1-434
5XM2X-ray2.19 ÅA/B=1-437
4Z2MX-ray2.98 ÅB=644-930
9EH2EM3.1 Åx=1-1047
9RZCEM3.66 Åk=1-1047
8YJMX-ray4.15 ÅA=644-988
8YJFX-ray4.4 ÅA=644-988
9GW2EM4.84 Åj=1-1047
6UPKEM4.9 ÅG=2-925
9S3GEM6.4 Åj=1-1047
9S0UEM6.72 Åk=1-1047
6UPLEM7.4 ÅG=2-925
9RZEEM8.53 Åj=1-1047

More AlphaFold highlights

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