9Q9P: TRIM21 PRYSPRY

TRIM21 PRYSPRY bound to compound 37. Determined by X-ray diffraction at 2.1 Å resolution. Released 8 Oct 2025.

Method
X-ray diffraction
Resolution
2.1 Å
Organism
Homo sapiens
Chains
1
Atoms
1,555
Mol. weight
23.05 kDa
Ligands
A1I4X
Released
8 Oct 2025

Explore 9Q9P in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9Q9P contains 4 α-helices and 17 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 B: 4 helices, 17 β-strands

ElementResiduesLengthSheet
α-helix0-23
β-strand311
β-strand812
β-strand17-1931
β-strand25-2841
β-strand48-4923
β-strand5012
β-strand5413
β-strand58-6471
β-strand71-7773
α-helix90-923
β-strand94-10073
β-strand104-10743
β-strand113-11423
β-strand123-12971
β-strand134-13961
α-helix140-1423
β-strand145-15061
β-strand159-16463
α-helix175-1762
β-strand177-17931

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
E3 ubiquitin-protein ligase TRIM21Bprotein198Homo sapiensP19474 (AlphaFold model)
Sequence of entity 1 (B), FASTA
>9Q9P_1 E3 ubiquitin-protein ligase TRIM21 (chains B)
MAHHHHHHMVHITLDPDTANPWLILSEDRRQVRLGDTQQSIPGNEERFDSYPMVLGAQHF
HSGKHYWEVDVTGKEAWDLGVCRDSVRRKGHFLLSSKSGFWTIWLWNKQKYEAGTYPQTP
LHLQVPPCQVGIFLDYEAGMVSFYNITDHGSLIYSFSECAFTGPLRPFFSPGFNDGGKNT
APLTLCPLNIGSQGSTDY

Ligands and cofactors

IDNameFormulaCopies
A1I4X(2~{S},4~{S})-1-[(3~{S})-3-azanyl-3-(2-methoxyphenyl)propanoyl]-4-cyclohexyl-~{…C30 H41 N5 O41

Primary citation

State-selective small molecule degraders that preferentially remove aggregates and oligomers. Luptak, J., Clift, D., Mukadam, A. et al. Nat Commun (2025) 16:10486-10486. DOI 10.1038/s41467-025-65454-z · PubMed

Other PDB entries of the same protein (UniProt P19474 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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