Structure of the TRIM25 coiled-coil. Determined by X-ray diffraction at 2.8 Å resolution. Released 10 Dec 2014.
Explore 4CFG in 3D Show helices and sheets RCSB PDB PDBe
4CFG contains 7 α-helices and 0 β-strands across 2 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 | 195-301 | 107 | |
| α-helix | 304-314 | 11 | |
| α-helix | 321-322 | 2 | |
| α-helix | 331-354 | 24 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 197-300 | 104 | |
| α-helix | 305-315 | 11 | |
| α-helix | 331-355 | 25 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| E3 UBIQUITIN/ISG15 ligase TRIM25 | A, B | protein | 630 | HOMO SAPIENS | Q14258 (AlphaFold model) |
>4CFG_1 E3 UBIQUITIN/ISG15 LIGASE TRIM25 (chains A, B) MAELCPLAEELSCSICLEPFKEPVTTPCGHNFCGSCLNETWAVQGSPYLCPQCRAVYQAR PQLHKNTVLCNVVEQFLQADLAREPPADVWTPPARASAPSPNAQVACDHCLKEAAVKTCL VCMASFCQEHLQPHFDSPAFQDHPLQPPVRDLLRRKCSQHNRLREFFCPEHSECICHICL VEHKTCSPASLSQASADLEATLRHKLTVMYSQINGASRALDDVRNRQQDVRMTANRKVEQ LQQEYTEMKALLDASETTSTRKIKEEEKRVNSQFDTIYQILLKKKSEIQTLKEEIEQSLT KRDEFEFLEKASKLRGISTQPVYIPEVELNHKLIKGIHQSTIDLKNELKQCIGRLQEPTP SSGDPGEHDPASTHKSTRPVKKVSKEEKKSKKPPPVPALPSKLPTFGAPEQLVDLKQAGL EAAAKATSSHPNSTSLKAKVLETFLAKSRPELLEYYIKVILDYNTAHNKVALSECYTVAS VAEMPQNYRPHPQRFTYCSQVLGLHCYKKGIHYWEVELQKNNFCGVGICYGSMNRQGPES RLGRNSASWCVEWFNTKISAWHNNVEKTLPSTKATRVGVLLNCDHGFVIFFAVADKVHLM YKFRVDFTEALYPAFWVFSAGATLSICSPK
Structure of the Trim25 Coiled-Coil. James, L. To be published.
Other PDB entries of the same protein (UniProt Q14258 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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