9Q9O: TRIM21 PRYSPRY

TRIM21 PRYSPRY bound to compound 36. Determined by X-ray diffraction at 2.46 Å resolution. Released 8 Oct 2025.

Method
X-ray diffraction
Resolution
2.46 Å
Organism
Homo sapiens
Chains
4
Atoms
6,064
Mol. weight
92.16 kDa
Ligands
A1I4Z
Released
8 Oct 2025

Explore 9Q9O in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9Q9O contains 14 α-helices and 63 β-strands across 4 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: 3 helices, 16 β-strands

ElementResiduesLengthSheet
α-helix0-23
β-strand314
β-strand815
β-strand17-1934
β-strand25-2844
β-strand48-4926
β-strand5015
β-strand5416
β-strand58-6474
β-strand71-7776
α-helix90-923
β-strand94-9966
β-strand105-10736
β-strand123-12974
β-strand134-13964
β-strand145-15064
β-strand159-16466
α-helix1761
β-strand177-17934
Chain B: 4 helices, 16 β-strands
ElementResiduesLengthSheet
α-helix0-23
β-strand311
β-strand812
β-strand17-1931
α-helix201
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-strand123-12971
β-strand134-13961
β-strand145-15061
β-strand159-16463
α-helix1761
β-strand177-17931
Chain C: 3 helices, 16 β-strands
ElementResiduesLengthSheet
α-helix0-23
β-strand317
β-strand818
β-strand17-1937
β-strand25-2847
β-strand48-4929
β-strand5018
β-strand5419
β-strand58-6477
β-strand71-7779
α-helix90-923
β-strand94-9969
β-strand105-10739
β-strand123-12977
β-strand134-13967
β-strand145-14957
β-strand159-16469
α-helix1761
β-strand177-17937
Chain D: 4 helices, 15 β-strands
ElementResiduesLengthSheet
α-helix0-23
β-strand3110
β-strand8-9211
β-strand17-19310
β-strand25-28410
β-strand48-50311
β-strand54111
β-strand58-64710
β-strand71-77711
α-helix90-923
β-strand94-100711
β-strand104-107411
β-strand123-129710
β-strand134-139610
α-helix140-1423
β-strand145-150610
β-strand159-164611
α-helix1761
β-strand177-179310

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
E3 ubiquitin-protein ligase TRIM21A, B, C, Dprotein198Homo sapiensP19474 (AlphaFold model)
Sequence of entity 1 (A, B, C, D), FASTA
>9Q9O_1 E3 ubiquitin-protein ligase TRIM21 (chains A, B, C, D)
MAHHHHHHMVHITLDPDTANPWLILSEDRRQVRLGDTQQSIPGNEERFDSYPMVLGAQHF
HSGKHYWEVDVTGKEAWDLGVCRDSVRRKGHFLLSSKSGFWTIWLWNKQKYEAGTYPQTP
LHLQVPPCQVGIFLDYEAGMVSFYNITDHGSLIYSFSECAFTGPLRPFFSPGFNDGGKNT
APLTLCPLNIGSQGSTDY

Ligands and cofactors

IDNameFormulaCopies
A1I4Z4-[[[4-imidazol-1-yl-3-[1-[(4-methoxyphenyl)methyl]-3-methyl-pyrazol-4-yl]pheny…C31 H32 N6 O24

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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