COP9 signalosome complex subunit 1 (GPS1) is a 491-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q13098.
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The mean pLDDT of this model is 84.6 (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 band | Meaning | Share of residues |
|---|---|---|
| Above 90 | Very high: backbone and side chains are usually accurate | 69% |
| 70 to 90 | Confident: backbone generally right | 15% |
| 50 to 70 | Low: treat with caution | 5% |
| Below 50 | Very low: often disordered regions | 12% |
What pLDDT means and how to read it
Essential component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2. The complex is also involved in phosphorylation of p53/TP53, c-jun/JUN, IkappaBalpha/NFKBIA, ITPK1 and IRF8/ICSBP, possibly via its association with CK2 and PKD kinases. CSN-dependent phosphorylation of TP53 and JUN promotes and protects degradation by the Ubl system, respectively. Suppresses G protein-…
Component of the CSN complex, composed of COPS1/GPS1, COPS2, COPS3, COPS4, COPS5, COPS6, COPS7 (COPS7A or COPS7B), COPS8 and COPS9 isoform 1 (PubMed:11337588, PubMed:18850735, PubMed:26456823). In the complex, it probably interacts directly with COPS2, COPS3, COPS4 and COPS5 (PubMed:11114242). Interacts directly with inositol kinase ITPK1 (PubMed:12324474). Interacts with CAPN8 (By similarity).…
Cytoplasm, Nucleus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 9QO4 | EM | 2.95 Å | A=1-491 |
| 9EFQ | EM | 2.96 Å | A=1-491 |
| 9PH4 | EM | 3.0 Å | A=1-491 |
| 9QO6 | EM | 3.0 Å | A=1-491 |
| 9EFV | EM | 3.03 Å | A=1-491 |
| 9EFM | EM | 3.16 Å | A=1-491 |
| 9QO1 | EM | 3.23 Å | A=1-491 |
| 9QO0 | EM | 3.26 Å | A=1-491 |
| 9E77 | EM | 3.3 Å | A=1-491 |
| 9E81 | EM | 3.3 Å | A=1-491 |
| 9EG8 | EM | 3.39 Å | A=1-491 |
| 9E5Z | EM | 3.4 Å | A=1-491 |
| 9EG1 | EM | 3.52 Å | A=1-491 |
| 4D10 | X-ray | 3.8 Å | A/I=12-491 |
| 9QO2 | EM | 3.8 Å | A=1-491 |
| 9EGL | EM | 3.93 Å | A=1-491 |
| 9QO5 | EM | 4.0 Å | A=1-491 |
| 4D18 | X-ray | 4.08 Å | A/I=12-491 |
| 8H38 | EM | 4.25 Å | A=12-491 |
| 9QO3 | EM | 4.6 Å | A=1-491 |
Showing 20 of 28 experimental structures (best resolution first).
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