9L8Y: HERC2

Crystal structure of HERC2. Determined by X-ray diffraction at 1.92 Å resolution. Released 5 Nov 2025.

Method
X-ray diffraction
Resolution
1.92 Å
Organism
Homo sapiens
Chains
1
Atoms
1,318
Mol. weight
18.35 kDa
Released
5 Nov 2025

Explore 9L8Y in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9L8Y contains 4 α-helices and 12 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: 4 helices, 12 β-strands

ElementResiduesLengthSheet
α-helix2554-25563
α-helix2560-257011
β-strand2576-257941
β-strand258312
β-strand258612
β-strand2591-259771
β-strand2607-261151
β-strand2616-262051
α-helix2622-26243
β-strand2625-262951
β-strand2644-264743
β-strand2667-267263
β-strand2678-268363
β-strand2686-269273
α-helix2693-26953
β-strand2696-269833

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
E3 ubiquitin-protein ligase HERC2Aprotein164Homo sapiensO95714
Sequence of entity 1 (A), FASTA
>9L8Y_1 E3 ubiquitin-protein ligase HERC2 (chains A)
GAMSTGAVVTESQTYKKRADFLSNDDYAVYVRENIQVGMMVRCCRAYEEVCEGDVGKVIK
LDRDGLHDLNVQCDWQQKGGTYWVRYIHVELIGYPPPSSSSHIKIGDKVRVKASVTTPKY
KWGSVTHQSVGVVKAFSANGKDIIVDFPQQSHWTGLLSEMELVP

Primary citation

Mechanistic insights into the iron-sulfur cluster-dependent interaction of the autophagy receptor NCOA4 with the E3 ligase HERC2. Liu, H., Shen, L., Gong, X. et al. Proc Natl Acad Sci U S A (2025) 122:e2510269122-e2510269122. DOI 10.1073/pnas.2510269122 · PubMed

Other PDB entries of the same protein (UniProt O95714), best resolution first:

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