5TTE: RBR E3 ubiquitin ligase

Crystal Structure of an RBR E3 ubiquitin ligase in complex with an E2-Ub thioester intermediate mimic. Determined by X-ray diffraction at 3.5 Å resolution. Released 23 Aug 2017.

Method
X-ray diffraction
Resolution
3.5 Å
Organisms
Homo sapiens, Triticum aestivum
Chains
3
Atoms
5,551
Mol. weight
94.08 kDa
Ligands
ZN
Released
23 Aug 2017

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

Secondary structure: helices and β-sheets

5TTE contains 27 α-helices and 32 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 B: 18 helices, 17 β-strands

ElementResiduesLengthSheet
β-strand102-10431
α-helix106-12419
α-helix128-13710
α-helix142-1509
α-helix154-1618
α-helix165-1684
β-strand183-18532
α-helix1861
β-strand192-19432
α-helix195-1973
β-strand198-20033
β-strand206-20833
α-helix209-22113
β-strand23014
β-strand23914
α-helix243-2464
α-helix252-26817
β-strand273-27531
β-strand284-28631
β-strand294-29635
β-strand302-30435
β-strand31015
α-helix317-32913
β-strand341-34336
β-strand350-35236
β-strand359-36137
β-strand370-37237
β-strand37817
α-helix403-43129
α-helix434-4385
α-helix444-4485
α-helix456-48025
α-helix486-50722
α-helix508-5125
α-helix518-54730
Chain E: 6 helices, 8 β-strands
ElementResiduesLengthSheet
α-helix6-1712
β-strand22-2768
β-strand34-3968
β-strand5019
β-strand51-5668
β-strand67-7048
β-strand79110
β-strand85110
α-helix88-903
α-helix101-11313
α-helix123-1319
α-helix133-14715
β-strand14919
α-helix150-1523
Chain F: 3 helices, 7 β-strands
ElementResiduesLengthSheet
β-strand1-6611
β-strand12-17611
β-strand22112
α-helix23-3412
α-helix38-403
β-strand42-45411
β-strand48-50311
β-strand55112
β-strand65-70611
α-helix71-733

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
E3 ubiquitin-protein ligase ARIH1Bprotein558Homo sapiensQ9Y4X5 (AlphaFold model)
Ubiquitin-conjugating enzyme E2 L3Eprotein167Homo sapiensP68036 (AlphaFold model)
ubiquitinFprotein86Triticum aestivumP69326 (AlphaFold model)
Sequence of entity 1 (B), FASTA
>5TTE_1 E3 ubiquitin-protein ligase ARIH1 (chains B)
SMDSDEGYNYEFDEDEECSEEDSGAEEEEDEDDDEPDDDTLDLGEVELVEPGLGVGGERD
GLLCGETGGGGGSALGPGGGGGGGGGGGGGGPGHEQEEDYRYEVLTAEQILQHMVECIRE
VNEVIQNPATITRILLSHFNWDKEKLMERYFDGNLEKLFAECHVINPSKKSRTRQMNTRS
SAQDMPCQICYLNYPNSYFTGLECGHKFCMQCWSEYLTTKIMEEGMGQTISCPAHGCDIL
VDDNTVMRLITDSKVKLKYQHLITNSFVECNRLLKWCPAPDCHHVVKVQYPDAKPVRCKC
GRQFCFNCGENWHDPVKCKWLKKWIKKCDDDSETSNWIAANTKECPKCHVTIEKDGGCNH
MVCRNQNCKAEFCWVCLGPWEPHGSAWYNCNRYNEDDAKAARDAQERSRAALQRYLFYCN
RYMNHMQSLRFEHKLYAQVKQKMEEMQQHNMSWIEVQFLKKAVDVLCQCRATLMYTYVFA
FYLKKNNQSIIFENNQADLENATEVLSGYLERDISQDSLQDIKQKVQDKYRYCESRRRVL
LQHVHEGYEKDLWEYIED
Sequence of entity 2 (E), FASTA
>5TTE_2 Ubiquitin-conjugating enzyme E2 L3 (chains E)
MAASRRLMKELEEIRKSGMKNFRNIQVDEANLLTWQGLIVPDNPPYDKGAFRIEINFPAE
YPFKPPKITFKTKIYHPNIDEKGQVKLPVISAENWKPATKTDQVIQSLIALVNDPQPEHP
LRADLAEEYSKDRKKFCKNAEEFTKKYGEKRPVDKLAAALEHHHHHH
Sequence of entity 3 (F), FASTA
>5TTE_3 ubiquitin (chains F)
MHHHHHHGSHMQIFVRTLTGRTITLEVESSDTIDNVRARIQDREGIPPDQQRLIFAGRQL
EDGRTLADYNIQRESTLHLVLRLRGG

Ligands and cofactors

IDNameFormulaCopies
ZNZinc ionZn6

Primary citation

Structural insights into the mechanism and E2 specificity of the RBR E3 ubiquitin ligase HHARI. Yuan, L., Lv, Z., Atkison, J.H. et al. Nat Commun (2017) 8:211-211. DOI 10.1038/s41467-017-00272-6 · PubMed

Other PDB entries of the same protein (UniProt Q9Y4X5 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

About this viewer

MolViewer shows 5TTE directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.