Glucocorticoid receptor (NR3C1) is a 777-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P04150.
Explore in 3D Color by confidence AlphaFold DB UniProt
The mean pLDDT of this model is 59.6 (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 band | Meaning | Share of residues |
|---|---|---|
| Above 90 | Very high: backbone and side chains are usually accurate | 35% |
| 70 to 90 | Confident: backbone generally right | 6% |
| 50 to 70 | Low: treat with caution | 4% |
| Below 50 | Very low: often disordered regions | 56% |
What pLDDT means and how to read it
Receptor for glucocorticoids (GC) (PubMed:27120390, PubMed:37478846). Has a dual mode of action: as a transcription factor that binds to glucocorticoid response elements (GRE), both for nuclear and mitochondrial DNA, and as a modulator of other transcription factors (PubMed:28139699). Affects inflammatory responses, cellular proliferation and differentiation in target tissues. Involved in chromatin remodeling (PubMed:9590696). Plays a role in rapid mRNA degradation by binding to the 5' UTR of target mRNAs and interacting with PNRC2 in a ligand-dependent manner which recruits the RNA helicase UPF1 and the mRNA-decapping enzyme DCP1A, leading to RNA decay (PubMed:25775514). Could act as a…
Heteromultimeric cytoplasmic complex with HSP90AA1, HSPA1A/HSPA1B, and FKBP5 or another immunophilin such as PPID, STIP1, or the immunophilin homolog PPP5C (PubMed:21730050). Upon ligand binding FKBP5 dissociates from the complex and FKBP4 takes its place, thereby linking the complex to dynein and mediating transport to the nucleus, where the complex dissociates (By similarity). Probably forms a…
Cytoplasm, Nucleus, Mitochondrion, Cytoplasm, cytoskeleton, spindle, Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, Chromosome, Nucleus, nucleoplasm
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 4UDD | X-ray | 1.8 Å | A=500-777 |
| 5E69 | X-ray | 1.85 Å | A/B=417-506 |
| 4HN5 | X-ray | 1.9 Å | A/B=417-506 |
| 4P6W | X-ray | 1.95 Å | A=526-777 |
| 8A9G | X-ray | 1.96 Å | C/D=518-530 |
| 5CBX | X-ray | 2.0 Å | A/B/E/F=412-495 |
| 5CBY | X-ray | 2.0 Å | A/B=412-495 |
| 6X6E | X-ray | 2.0 Å | A/B=417-491 |
| 5UC3 | X-ray | 2.01 Å | A/B=522-777 |
| 6YMO | X-ray | 2.02 Å | C/D=611-623 |
| 6YO8 | X-ray | 2.09 Å | E/F/G/H=518-530 |
| 3K22 | X-ray | 2.1 Å | A/B=521-777 |
| 5NFP | X-ray | 2.1 Å | A=500-777 |
| 8VKZ | X-ray | 2.13 Å | A/B=528-777 |
| 3E7C | X-ray | 2.15 Å | A/B=521-777 |
| 5VA7 | X-ray | 2.15 Å | A/B=419-488 |
| 6EL7 | X-ray | 2.18 Å | A=500-777 |
| 6EL9 | X-ray | 2.19 Å | A=500-777 |
| 5CBZ | X-ray | 2.2 Å | A/B/E/F=412-495 |
| 5E6A | X-ray | 2.2 Å | A/B=417-506 |
Showing 20 of 58 experimental structures (best resolution first).
MolViewer loads the AlphaFold model straight from AlphaFold DB into your browser. Show it as a cartoon, color by pLDDT, measure distances and angles, and load a PDB structure next to it to compare.