32QL: Human TRIM21 PRYSPRY domain

Human TRIM21 PRYSPRY domain in complex with HGC652. Determined by X-ray diffraction at 1.4 Å resolution. Released 29 Jul 2026.

Method
X-ray diffraction
Resolution
1.4 Å
Organism
Homo sapiens
Chains
1
Atoms
1,557
Mol. weight
21.37 kDa
Ligands
A1KED
Released
29 Jul 2026

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

Secondary structure: helices and β-sheets

32QL 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
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
β-strand428-43362
β-strand442-44763
α-helix458-4592
β-strand460-46232

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
E3 ubiquitin-protein ligase TRIM21Aprotein181Homo sapiensP19474 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>32QL_1 E3 ubiquitin-protein ligase TRIM21 (chains A)
SMVHITLDPDTANPWLILSEDRRQVRLGDTQQSIPGNEERFDSYPMVLGAQHFHSGKHYW
EVDVTGKEAWDLGVCRDSVRRKGHFLLSSKSGFWTIWLWNKQKYEAGTYPQTPLHLQVPP
CQVGIFLDYEAGMVSFYNITDHGSLIYSFSECAFTGPLRPFFSPGFNDGGKNTAPLTLCP
L

Ligands and cofactors

IDNameFormulaCopies
A1KED~{N}-(cyclohexylmethyl)-4-(4-fluoranyl-2-methylsulfanyl-phenyl)-~{N}-methyl-2-m…C23 H28 F N O3 S21

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

Primary citation

Human TRIM21 PRYSPRY domain in complex with HGC652. Kim, Y., Lucic, A., 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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