P32597: Nuclear protein STH1/NPS1 (STH1)

Nuclear protein STH1/NPS1 (STH1) is a 1359-residue protein from Saccharomyces cerevisiae (strain ATCC 204508 / S288c). This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P32597.

Gene
STH1
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Length
1359 residues
Mean pLDDT
70.6
Model
AF-P32597-F1 v6
Model created
1 Aug 2025
PDB structures
15

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Model confidence (pLDDT)

The mean pLDDT of this model is 70.6 (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 accurate20%
70 to 90Confident: backbone generally right43%
50 to 70Low: treat with caution15%
Below 50Very low: often disordered regions22%

What pLDDT means and how to read it

Function

Catalytic component of the chromatin structure-remodeling complex (RSC), which is involved in transcription regulation and nucleosome positioning. RSC is responsible for the transfer of a histone octamer from a nucleosome core particle to naked DNA. The reaction requires ATP and involves an activated RSC-nucleosome intermediate. Remodeling reaction also involves DNA translocation, DNA twist and conformational change. As a reconfigurer of centromeric and flanking nucleosomes, RSC complex is required both for proper kinetochore function in chromosome segregation and, via a PKC1-dependent signaling pathway, for organization of the cellular cytoskeleton. This subunit is the essential ATPase of…

Subunit structure

Interacts directly with SFH1, CSE4, histones H3, H4 and H2B, and via its N-terminus, with RSC8. Interacts with LDB7, NPL6 and RTT102. Component of the two forms of the RSC complex composed of at least either RSC1 or RSC2, and ARP7, ARP9, LDB7, NPL6, RSC3, RSC30, RSC4, RSC58, RSC6, RSC8, RSC9, SFH1, STH1, HTL1 and probably RTT102. The complexes interact with histone and histone variant components…

Subcellular location

Nucleus

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
6KMJX-ray1.4 ÅA=1248-1359
7F3SX-ray1.4 ÅA=1248-1359
6UY1X-ray2.21 ÅA/B/C/D/E/F/G/H=1250-1359
6KMBX-ray2.4 ÅA/B/C/D=1248-1359
6MR4X-ray2.71 ÅA/B/C/D/E/F=1250-1359
6V8OEM3.07 ÅR=1-1359
6K15EM3.4 ÅJ=1-1359
6VZ4EM3.9 ÅK=301-1097
6VZGEM4.2 ÅK=301-1097
6KW3EM7.13 ÅJ/W/Y=1-1359
6KW4EM7.55 ÅJ/V/Y=1-1359
6KW5EM10.13 ÅJ/P/Q=1-1359
6TDAEM15.0 ÅS=1-1359
6V92EM20.0 ÅR=1-1359
6LQZNMRB=1183-1240

More AlphaFold highlights

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