9II5: Human TRIM21 PRYSPRY

Crystal structure of human TRIM21 PRYSPRY in complex with compound 1. Determined by X-ray diffraction at 1.49 Å resolution. Released 7 May 2025.

Method
X-ray diffraction
Resolution
1.49 Å
Organism
Homo sapiens
Chains
1
Atoms
1,549
Mol. weight
20.64 kDa
Ligands
A1D9F
Released
7 May 2025

Explore 9II5 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9II5 contains 3 α-helices and 16 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, 16 β-strands

ElementResiduesLengthSheet
β-strand29111
α-helix293-2953
β-strand300-30232
β-strand308-31142
α-helix318-3203
β-strand331-33223
β-strand33311
β-strand33713
β-strand341-34772
β-strand354-36073
β-strand377-38263
β-strand388-39033
β-strand396-39833
β-strand406-41272
β-strand417-42262
β-strand428-43362
β-strand442-44763
α-helix458-4592
β-strand460-46232

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
E3 ubiquitin-protein ligase TRIM21Aprotein178Homo sapiensP19474 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>9II5_1 E3 ubiquitin-protein ligase TRIM21 (chains A)
VHITLDPDTANPWLILSEDRRQVRLGDTQQSIPGNEERFDSYPMVLGAQHFHSGKHYWEV
DVTGKEAWDLGVCRDSVRRKGHFLLSSKSGFWTIWLWNKQKYEAGTYPQTPLHLQVPPCQ
VGIFLDYEAGMVSFYNITDHGSLIYSFSECAFTGPLRPFFSPGFNDGGKNTAPLTALC

Ligands and cofactors

IDNameFormulaCopies
A1D9F~{N}-[(1-fluoranylcyclohexyl)methyl]-~{N}-methyl-4-(2-methylsulfanylphenyl)-2-m…C23 H28 F N O3 S21

Primary citation

Chemically Induced Nuclear Pore Complex Protein Degradation via TRIM21. Li, X., Wang, Q., Guo, A. et al. ACS Chem Biol (2025) 20:1020-1028. DOI 10.1021/acschembio.4c00833 · 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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