9Q88: RNF38 RING domain

High-resolution structure of RNF38 RING domain. Determined by X-ray diffraction at 1.2 Å resolution. Released 30 Jul 2025.

Method
X-ray diffraction
Resolution
1.2 Å
Organism
Homo sapiens
Chains
1
Atoms
741
Mol. weight
9.27 kDa
Ligands
ZN
Released
30 Jul 2025

Explore 9Q88 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9Q88 contains 3 α-helices and 7 β-strands across 1 chain. 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: 3 helices, 7 β-strands

ElementResiduesLengthSheet
α-helix392-3943
α-helix396-3972
β-strand398-40031
β-strand412-41322
β-strand418-41922
β-strand425-42841
β-strand434-43631
α-helix437-44711
β-strand44913
β-strand45613

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
E3 ubiquitin-protein ligase RNF38Aprotein79Homo sapiensQ9H0F5 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>9Q88_1 E3 ubiquitin-protein ligase RNF38 (chains A)
GSTKADIEQLPSYRFNPNNHQSEQTLCVVCMCDFESRQLLRVLPCNHEFHAKCVDKWLKA
NRTCPICRADASEVHRDSE

Ligands and cofactors

IDNameFormulaCopies
ZNZinc ionZn2

Primary citation

Tuning ubiquitin transfer by RING E3 ubiquitin ligases through the linchpin residue. Nakasone, M.A., Buetow, L., Gabrielsen, M. et al. Life Sci Alliance (2025) 8. DOI 10.26508/lsa.202503394 · 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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