6FLN: Human TRIM25 coiled-coil and PRYSPRY domains

Crystal structure of the human TRIM25 coiled-coil and PRYSPRY domains. Determined by X-ray diffraction at 3.6 Å resolution. Released 23 May 2018.

Method: X-ray diffraction
Resolution: 3.6 Å
Organism: Homo sapiens
Chains: 3
Atoms: 8,861
Mol. weight: 150.87 kDa
Released: 23 May 2018

Explore 6FLN in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6FLN contains 30 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.

Chain A: 10 helices, 17 β-strands

Element	Residues	Length	Sheet
α-helix	192-300	109
α-helix	307-312	6
α-helix	313-315	3
α-helix	331-356	26
α-helix	437-445	9
α-helix	449-452	4
α-helix	453-455	3
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	558-562	5	3
β-strand	566-568	3	3
α-helix	569-571	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	623-627	5	1

Chain B: 10 helices, 17 β-strands

Element	Residues	Length	Sheet
α-helix	192-300	109
α-helix	307-312	6
α-helix	313-315	3
α-helix	331-356	26
α-helix	435-445	11
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	511-519	9	4
β-strand	523-530	8	6
α-helix	538-540	3
β-strand	548-554	7	6
β-strand	558-562	5	6
β-strand	566-568	3	6
α-helix	569-571	3
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	623-627	5	4

Chain E: 10 helices, 17 β-strands

Element	Residues	Length	Sheet
α-helix	192-300	109
α-helix	307-312	6
α-helix	313-315	3
α-helix	331-355	25
α-helix	435-445	11
α-helix	449-452	4
α-helix	453-455	3
β-strand	456	1	7
β-strand	461	1	8
β-strand	470-473	4	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	511-519	9	7
β-strand	523-530	8	9
α-helix	538-540	3
β-strand	548-554	7	9
β-strand	558-562	5	9
β-strand	566-568	3	9
α-helix	569-571	3
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	623-627	5	7

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
E3 ubiquitin/ISG15 ligase TRIM25	A, B, E	protein	445	Homo sapiens	Q14258 (AlphaFold model)

Sequence of entity 1 (A, B, E), FASTA

>6FLN_1 E3 ubiquitin/ISG15 ligase TRIM25 (chains A, B, E)
GAMASLSQASADLEATLRHKLTVMYSQINGASRALDDVRNRQQDVRMTANRKVEQLQQEY
TEMKALLDASETTSTRKIKEEEKRVNSKFDTIYQILLKKKSEIQTLKEEIEQSLTKRDEF
EFLEKASKLRGISTKPVYIPEVELNHKLIKGIHQSTIDLKNELKQCIGRLQEPTPSSGDP
GEHDPASTHKSTRPVKKVSKEEKKSKKPPPVPALPSKLPTFGAPEQLVDLKQAGLEAAAK
ATSSHPNSTSLKAKVLETFLAKSRPELLEYYIKVILDYNTAHNKVALSECYTVASVAEMP
QNYRPHPQRFTYCSQVLGLHCYKKGIHYWEVELQKNNFCGVGICYGSMNRQGPESRLGRN
SASWCVEWFNTKISAWHNNVEKTLPSTKATRVGVLLNCDHGFVIFFAVADKVHLMYKFRV
DFTEALYPAFWVFSAGATLSICSPK

Primary citation

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:

9I0T 1.8 Å, Crystal structure of TRIM25 PRYSPRY covalently bound to…
6FLM 2.01 Å, Crystal structure of the human TRIM25 PRYSPRY domain
5FER 2.34 Å, Complex of TRIM25 RING with UbcH5-Ub
5EYA 2.4 Å, TRIM25 RING domain in complex with Ubc13-Ub conjugate
4LTB 2.59 Å, Coiled-coil domain of TRIM25
9IUN 2.7 Å, Crystal structure of Trim25 Pspry
4CFG 2.8 Å, Structure of the TRIM25 coiled-coil
5NT1 2.82 Å, Complex of influenza A NS1 effector domain with TRIM25 coiled coil
5NT2 4.26 Å, Complex of influenza A NS1 with TRIM25 coiled coil domain

Browse structure collections

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