P32835: GTP-binding nuclear protein GSP1/CNR1 (GSP1)

GTP-binding nuclear protein GSP1/CNR1 (GSP1) is a 219-residue protein from Saccharomyces cerevisiae (strain ATCC 204508 / S288c). This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P32835.

Gene
GSP1
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Length
219 residues
Mean pLDDT
88.7
Model
AF-P32835-F1 v6
Model created
1 Aug 2025
PDB structures
14

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Model confidence (pLDDT)

The mean pLDDT of this model is 88.7 (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 accurate72%
70 to 90Confident: backbone generally right19%
50 to 70Low: treat with caution5%
Below 50Very low: often disordered regions5%

What pLDDT means and how to read it

Function

GTP-binding protein involved in nucleocytoplasmic transport. Required for the import of protein into the nucleus and also for RNA export. By analogy with Ras, Ran may be activated when GTP is exchanged for bound GDP by RCC1 and inactivated when GTP is hydrolyzed by Ran upon activation by RanGAP1. Also participates in nucleosome assembly by stimulating the release of histone H2A-H2B dimers from their nuclear import chaperone KAP114, to facilitate their deposition into nucleosomes by NAP1 (PubMed:39601790)

Subunit structure

Found in a nuclear export complex with RanGTP, exportin and pre-miRNA (By similarity). Forms a complex with YRB1 (PubMed:10921930). Interacts with NAP1; for the nuclear import of histone H2A-H2B dimers and their assembly into nucleosomes (PubMed:39601790). Interacts with histones H2A and H2B; for the nuclear import of histone H2A-H2B dimers and their assembly into nucleosomes (PubMed:39601790).…

Subcellular location

Nucleus

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
3M1IX-ray2.0 ÅA=1-219
3WYGX-ray2.15 ÅA=1-182
2X19X-ray2.8 ÅA=8-179
9B3IEM2.88 ÅD=2-179
8QYZX-ray3.0 ÅA/B/E/G=1-182
9D45EM3.1 ÅB=2-179
9DZ6EM3.1 ÅB=2-179
3ICQX-ray3.2 ÅB/C=9-179
9DXMEM3.2 ÅB=2-179
9OGBEM3.25 ÅB=1-179
8F1EEM3.28 ÅD=1-179
8F19EM3.49 ÅB=1-179
8F7AEM3.78 ÅB=1-219
8DYOEM7.1 ÅB=1-219

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