7OJX: E3 ubiquitin-protein ligase RNF38

E2 UBE2K covalently linked to donor Ub, acceptor di-Ub, and RING E3 primed for K48-linked Ub chain synthesis. Determined by X-ray diffraction at 2.4 Å resolution. Released 12 Jan 2022.

Method
X-ray diffraction
Resolution
2.4 Å
Organism
Homo sapiens
Chains
5
Atoms
3,739
Mol. weight
57.99 kDa
Ligands
ZN, ME7
Released
12 Jan 2022

Explore 7OJX in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7OJX contains 20 α-helices and 38 β-strands across 5 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: 2 helices, 7 β-strands

ElementResiduesLengthSheet
β-strand398-40031
β-strand412-41322
β-strand418-41922
α-helix4241
β-strand425-42841
β-strand434-43631
α-helix437-44610
β-strand44913
β-strand45613
Chain B: 10 helices, 9 β-strands
ElementResiduesLengthSheet
α-helix5-1612
β-strand27-3154
β-strand38-4474
α-helix45-462
β-strand55-6174
α-helix70-712
β-strand72-7544
β-strand8115
β-strand8415
β-strand9014
β-strand9115
β-strand9316
α-helix94-963
α-helix106-11712
α-helix128-1369
α-helix138-15316
α-helix160-17112
α-helix176-18510
α-helix190-1989
Chain C: 3 helices, 8 β-strands
ElementResiduesLengthSheet
β-strand2-657
β-strand12-1657
β-strand2218
α-helix23-3412
α-helix38-403
β-strand41-4557
β-strand48-4927
α-helix50-512
β-strand5518
β-strand66-7167
β-strand7516
Chain D: 4 helices, 7 β-strands
ElementResiduesLengthSheet
β-strand2-769
β-strand12-1659
β-strand22110
α-helix23-3412
α-helix38-403
β-strand41-4559
β-strand48-4929
α-helix50-512
β-strand55110
α-helix57-593
β-strand66-7169
Chain E: 1 helix, 7 β-strands
ElementResiduesLengthSheet
β-strand2-6511
β-strand12-16511
β-strand22112
α-helix23-3412
β-strand41-45511
β-strand48-49211
β-strand55112
β-strand66-71611

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
E3 ubiquitin-protein ligase RNF38Aprotein79Homo sapiensQ9H0F5 (AlphaFold model)
Ubiquitin-conjugating enzyme E2 KBprotein202Homo sapiensP61086 (AlphaFold model)
Polyubiquitin-BCprotein79Homo sapiensP0CG47 (AlphaFold model)
Polyubiquitin-BDprotein76Homo sapiensP0CG47 (AlphaFold model)
Polyubiquitin-BEprotein76Homo sapiensP0CG47 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>7OJX_1 E3 ubiquitin-protein ligase RNF38 (chains A)
GSTKADIEQLPSYRFNPNNHQSEQTLCVVCMCDFESRQLLRVLPCNHEFHAKCVDKWLKA
NRTCPICRADASEVHRDSE
Sequence of entity 2 (B), FASTA
>7OJX_2 Ubiquitin-conjugating enzyme E2 K (chains B)
GSMANIAVQRIKREFKEVLKSEETSKNQIKVDLVDENFTELRGEIAGPPDTPYEGGRYQL
EIKIPETYPFNPPKVRFITKIWHPNISSVTGAIKLDILRDQWAAAMTLRTVLLSLQALLA
AAEPDCPQDAVVANQYKQNPEMFKQTARLWAHVYAGAPVSSPEYTKKIENLSAMGFDRNA
VIVALSSKSWDVETATELLLSN
Sequence of entity 3 (C), FASTA
>7OJX_3 Polyubiquitin-B (chains C)
GGSMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLS
DYNIQKESTLHLVLRLRGG
Sequence of entity 4 (D), FASTA
>7OJX_4 Polyubiquitin-B (chains D)
MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGCQLEDGRTLSDYN
IQKESTLHLVLRLRGG
Sequence of entity 5 (E), FASTA
>7OJX_5 Polyubiquitin-B (chains E)
MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYN
IQKESTLHLVLRLRGG

Ligands and cofactors

IDNameFormulaCopies
ZNZinc ionZn2
ME71,1'-ethane-1,2-diylbis(1H-pyrrole-2,5-dione)C10 H8 N2 O41

Primary citation

Structure of UBE2K-Ub/E3/polyUb reveals mechanisms of K48-linked Ub chain extension. Nakasone, M.A., Majorek, K.A., Gabrielsen, M. et al. Nat Chem Biol (2022) 18:422-431. DOI 10.1038/s41589-021-00952-x · PubMed

Other PDB entries of the same protein (UniProt Q9H0F5 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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