32QM: Human TRIM21 PRYSPRY domain

Human TRIM21 PRYSPRY domain in complex with compound 5 (Z31). Determined by X-ray diffraction at 1.5 Å resolution. Released 29 Jul 2026.

Method
X-ray diffraction
Resolution
1.5 Å
Organism
Homo sapiens
Chains
1
Atoms
1,564
Mol. weight
21.08 kDa
Ligands
A1KEE
Released
29 Jul 2026

Explore 32QM in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

32QM contains 5 α-helices and 18 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: 5 helices, 18 β-strands

ElementResiduesLengthSheet
β-strand29111
α-helix293-2953
β-strand300-30232
β-strand308-31142
β-strand331-33223
β-strand33311
β-strand33713
β-strand341-34772
β-strand354-36073
α-helix373-3753
β-strand377-38373
β-strand387-39043
β-strand396-39833
β-strand406-41272
β-strand417-42262
α-helix423-4253
β-strand428-43362
β-strand442-44763
β-strand45214
β-strand45514
α-helix458-4592
β-strand460-46232
α-helix463-4642

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
E3 ubiquitin-protein ligase TRIM21Aprotein181Homo sapiensP19474 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>32QM_1 E3 ubiquitin-protein ligase TRIM21 (chains A)
SMVHITLDPDTANPWLILSEDRRQVRLGDTQQSIPGNEERFDSYPMVLGAQHFHSGKHYW
EVDVTGKEAWDLGVCRDSVRRKGHFLLSSKSGFWTIWLWNKQKYEAGTYPQTPLHLQVPP
CQVGIFLDYEAGMVSFYNITDHGSLIYSFSECAFTGPLRPFFSPGFNDGGKNTAPLTLCP
L

Ligands and cofactors

IDNameFormulaCopies
A1KEE~{N}-[(1~{R})-1-cyclohexylethyl]-4-(4-fluoranyl-2-methylsulfanyl-phenyl)-~{N}-m…C24 H30 F N O3 S21

Water and common crystallization additives (EDO) are not listed.

Primary citation

Human TRIM21 PRYSPRY domain in complex with compound 5 (Z31). Kim, Y., Schallmayer, L., Knapp, S. et al. To be published.

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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