5EYA: TRIM25 RING domain

TRIM25 RING domain in complex with Ubc13-Ub conjugate. Determined by X-ray diffraction at 2.4 Å resolution. Released 17 Aug 2016.

Method
X-ray diffraction
Resolution
2.4 Å
Organism
Homo sapiens
Chains
6
Atoms
5,018
Mol. weight
70.79 kDa
Ligands
ZN
Released
17 Aug 2016

Explore 5EYA in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5EYA contains 27 α-helices and 48 β-strands across 6 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.

Chains A and B: 8 helices, 9 β-strands

ElementResiduesLengthSheet
α-helix6-1712
α-helix19-202
β-strand23-2861
β-strand31-40101
α-helix41-422
β-strand51-5771
α-helix66-672
β-strand68-7141
β-strand7712
β-strand8012
β-strand8511
β-strand8612
β-strand8813
α-helix89-913
α-helix101-11313
α-helix123-1319
α-helix133-14715
Chain C: 3 helices, 8 β-strands
ElementResiduesLengthSheet
β-strand2-6513
α-helix111
β-strand12-16513
β-strand22114
α-helix23-3412
β-strand41-45513
β-strand48-49213
β-strand55114
α-helix57-593
β-strand66-71613
β-strand75112
Chain D: 2 helices, 8 β-strands
ElementResiduesLengthSheet
β-strand2-6515
β-strand12-16515
β-strand22116
α-helix23-3412
α-helix38-403
β-strand41-45515
β-strand48-49215
β-strand55116
β-strand66-71615
β-strand7513
Chain F: 3 helices, 7 β-strands
ElementResiduesLengthSheet
α-helix7-104
β-strand1214
β-strand1914
β-strand23-2535
β-strand31-3335
α-helix34-4310
β-strand48-4926
β-strand56-5726
β-strand6515
α-helix67-8014
Chain G: 3 helices, 7 β-strands
ElementResiduesLengthSheet
α-helix2-76
β-strand1217
β-strand1917
β-strand23-2538
β-strand31-3338
α-helix34-4310
β-strand48-4929
β-strand56-5729
β-strand6518
α-helix67-7812

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Ubiquitin-conjugating enzyme E2 NA, Bprotein152Homo sapiensP61088 (AlphaFold model)
Tripartite motif-containing 25 variantF, Gprotein86Homo sapiensQ14258 (AlphaFold model)
Polyubiquitin-BC, Dprotein76Homo sapiensP0CG47 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>5EYA_1 Ubiquitin-conjugating enzyme E2 N (chains A, B)
MAGLPRRIIKETQRLLAEPVPGIKAEPDESNARYFHVVIAGPQDSPFEGGTFKLELFLPE
EYPMAAPKVRFMTKIYHPNVDKLGRIKLDILKDKWSPALQIRTVLLSIQALLSAPNPDDP
LANDVAEQWKTNEAQAIETARAWTRLYAMNNI
Sequence of entity 2 (F, G), FASTA
>5EYA_2 Tripartite motif-containing 25 variant (chains F, G)
GSHMAELCPLAEELSCSICLEPFKEPVTTPCGHNFCGSCLNETWAVQGSPYLCPQCRAVY
QARPQLHKNTVLCNVVEQFLQADLAR
Sequence of entity 3 (C, D), FASTA
>5EYA_3 Polyubiquitin-B (chains C, D)
MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYN
IQKESTLHLVLRLRGG

Ligands and cofactors

IDNameFormulaCopies
ZNZinc ionZn4

Primary citation

Mechanism of TRIM25 Catalytic Activation in the Antiviral RIG-I Pathway. Sanchez, J.G., Chiang, J.J., Sparrer, K.M. et al. Cell Rep (2016) 16:1315-1325. DOI 10.1016/j.celrep.2016.06.070 · PubMed

Other PDB entries of the same protein (UniProt P61088 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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