Crystal structure of the human TRIM25 PRYSPRY domain. Determined by X-ray diffraction at 2.01 Å resolution. Released 23 May 2018.
Explore 6FLM in 3D Show helices and sheets RCSB PDB PDBe
6FLM contains 14 α-helices and 51 β-strands across 3 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 433-445 | 13 | |
| α-helix | 449-453 | 5 | |
| β-strand | 456 | 1 | 1 |
| β-strand | 461 | 1 | 2 |
| β-strand | 470-473 | 4 | 1 |
| β-strand | 478-481 | 4 | 1 |
| α-helix | 488-490 | 3 | |
| β-strand | 500-502 | 3 | 3 |
| β-strand | 503 | 1 | 2 |
| β-strand | 507 | 1 | 3 |
| β-strand | 511-519 | 9 | 1 |
| β-strand | 523-530 | 8 | 3 |
| α-helix | 538-540 | 3 | |
| β-strand | 548-554 | 7 | 3 |
| β-strand | 557-562 | 6 | 3 |
| β-strand | 565-568 | 4 | 3 |
| β-strand | 576-582 | 7 | 1 |
| β-strand | 587-593 | 7 | 1 |
| β-strand | 597-604 | 8 | 1 |
| β-strand | 611-617 | 7 | 3 |
| β-strand | 623-626 | 4 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 434-445 | 12 | |
| α-helix | 449-452 | 4 | |
| α-helix | 453-455 | 3 | |
| β-strand | 456 | 1 | 4 |
| β-strand | 461 | 1 | 5 |
| β-strand | 470-473 | 4 | 4 |
| β-strand | 478-481 | 4 | 4 |
| α-helix | 488-490 | 3 | |
| β-strand | 500-502 | 3 | 6 |
| β-strand | 503 | 1 | 5 |
| β-strand | 507 | 1 | 6 |
| β-strand | 511-518 | 8 | 4 |
| β-strand | 523-530 | 8 | 6 |
| α-helix | 538-540 | 3 | |
| β-strand | 548-554 | 7 | 6 |
| β-strand | 557-562 | 6 | 6 |
| β-strand | 565-568 | 4 | 6 |
| β-strand | 576-582 | 7 | 4 |
| β-strand | 587-593 | 7 | 4 |
| β-strand | 597-604 | 8 | 4 |
| β-strand | 611-617 | 7 | 6 |
| β-strand | 623-626 | 4 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 433-445 | 13 | |
| α-helix | 449-452 | 4 | |
| α-helix | 453-455 | 3 | |
| β-strand | 456 | 1 | 7 |
| β-strand | 461 | 1 | 8 |
| β-strand | 470-472 | 3 | 7 |
| β-strand | 478-481 | 4 | 7 |
| α-helix | 488-490 | 3 | |
| β-strand | 500-502 | 3 | 9 |
| β-strand | 503 | 1 | 8 |
| β-strand | 507 | 1 | 9 |
| β-strand | 511-518 | 8 | 7 |
| β-strand | 524-530 | 7 | 9 |
| α-helix | 538-540 | 3 | |
| β-strand | 548-554 | 7 | 9 |
| β-strand | 557-562 | 6 | 9 |
| β-strand | 565-568 | 4 | 9 |
| β-strand | 576-582 | 7 | 7 |
| β-strand | 587-593 | 7 | 7 |
| β-strand | 597-604 | 8 | 7 |
| β-strand | 611-617 | 7 | 9 |
| β-strand | 623-626 | 4 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| E3 ubiquitin/ISG15 ligase TRIM25 | A, B, C | protein | 199 | Homo sapiens | Q14258 (AlphaFold model) |
>6FLM_1 E3 ubiquitin/ISG15 ligase TRIM25 (chains A, B, C) GMASLKAKVLETFLAKSRPELLEYYIKVILDYNTAHNKVALSECYTVASVAEMPQNYRPH PQRFTYCSQVLGLHCYKKGIHYWEVELQKNNFCGVGICYGSMNRQGPESRLGRNSASWCV EWFNTKISAWHNNVEKTLPSTKATRVGVLLNCDHGFVIFFAVADKVHLMYKFRVDFTEAL YPAFWVFSAGATLSICSPK
Molecular mechanism of influenza A NS1-mediated TRIM25 recognition and inhibition. Koliopoulos, M.G., Lethier, M., van der Veen, A.G. et al. Nat Commun (2018) 9:1820-1820. DOI 10.1038/s41467-018-04214-8 · PubMed
Other PDB entries of the same protein (UniProt Q14258 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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