21EE: Human PHF20L1(1-80)

Crystal structure of human PHF20L1(1-80) in complex with H3K36me. Determined by X-ray diffraction at 1.34 Å resolution. Released 12 Aug 2026.

Method
X-ray diffraction
Resolution
1.34 Å
Organism
Homo sapiens
Chains
2
Atoms
717
Mol. weight
11.51 kDa
Released
12 Aug 2026

Explore 21EE in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

21EE contains 2 α-helices and 5 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: 2 helices, 5 β-strands

ElementResiduesLengthSheet
α-helix4-63
β-strand18-2251
β-strand28-37101
β-strand42-4761
α-helix52-543
β-strand56-5941
β-strand65-6621

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
PHD finger protein 20-like protein 1Aprotein80Homo sapiensA8MW92 (AlphaFold model)
Histone H3.1tBprotein15Homo sapiensQ16695 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>21EE_1 PHD finger protein 20-like protein 1 (chains A)
MSKKPPNRPGITFEIGARLEALDYLQKWYPSRIEKIDYEEGKMLVHFERWSHRYDEWIYW
DSNRLRPLERPALRKEGLKD
Sequence of entity 2 (B), FASTA
>21EE_2 Histone H3.1t (chains B)
SAPATGGVKKPHRYR

Primary citation

A revised model for PHF20L1 Tudor function: DNA binding overrides methylation selectivity on nucleosomes. Huang, X., Xiao, Q., Liu, X. et al. J Biol Chem (2026) 302:113181-113181. DOI 10.1016/j.jbc.2026.113181 · PubMed

Other PDB entries of the same protein (UniProt A8MW92 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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