4CFG: TRIM25 coiled-coil

Structure of the TRIM25 coiled-coil. Determined by X-ray diffraction at 2.8 Å resolution. Released 10 Dec 2014.

Method
X-ray diffraction
Resolution
2.8 Å
Organism
HOMO SAPIENS
Chains
2
Atoms
2,669
Mol. weight
142.9 kDa
Released
10 Dec 2014

Explore 4CFG in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 4 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix195-301107
α-helix304-31411
α-helix321-3222
α-helix331-35424
Chain B: 3 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix197-300104
α-helix305-31511
α-helix331-35525

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
E3 UBIQUITIN/ISG15 ligase TRIM25A, Bprotein630HOMO SAPIENSQ14258 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>4CFG_1 E3 UBIQUITIN/ISG15 LIGASE TRIM25 (chains A, B)
MAELCPLAEELSCSICLEPFKEPVTTPCGHNFCGSCLNETWAVQGSPYLCPQCRAVYQAR
PQLHKNTVLCNVVEQFLQADLAREPPADVWTPPARASAPSPNAQVACDHCLKEAAVKTCL
VCMASFCQEHLQPHFDSPAFQDHPLQPPVRDLLRRKCSQHNRLREFFCPEHSECICHICL
VEHKTCSPASLSQASADLEATLRHKLTVMYSQINGASRALDDVRNRQQDVRMTANRKVEQ
LQQEYTEMKALLDASETTSTRKIKEEEKRVNSQFDTIYQILLKKKSEIQTLKEEIEQSLT
KRDEFEFLEKASKLRGISTQPVYIPEVELNHKLIKGIHQSTIDLKNELKQCIGRLQEPTP
SSGDPGEHDPASTHKSTRPVKKVSKEEKKSKKPPPVPALPSKLPTFGAPEQLVDLKQAGL
EAAAKATSSHPNSTSLKAKVLETFLAKSRPELLEYYIKVILDYNTAHNKVALSECYTVAS
VAEMPQNYRPHPQRFTYCSQVLGLHCYKKGIHYWEVELQKNNFCGVGICYGSMNRQGPES
RLGRNSASWCVEWFNTKISAWHNNVEKTLPSTKATRVGVLLNCDHGFVIFFAVADKVHLM
YKFRVDFTEALYPAFWVFSAGATLSICSPK

Primary citation

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:

Browse structure collections

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