9FE1: Ternary DARPin NY_1/HLA-A0201/NY-ESO1 complex

Cryo-EM structure of the ternary DARPin NY_1/HLA-A0201/NY-ESO1 complex. Determined by electron microscopy at 3.1 Å resolution. Released 28 May 2025.

Method
Electron microscopy
Resolution
3.1 Å
Organisms
Homo sapiens, synthetic construct
Chains
4
Atoms
4,295
Mol. weight
65.11 kDa
Released
28 May 2025

Explore 9FE1 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9FE1 contains 16 α-helices and 29 β-strands across 3 chains. 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: 6 helices, 18 β-strands

ElementResiduesLengthSheet
β-strand3-12101
β-strand21-2881
β-strand31-3771
α-helix52-543
α-helix57-8428
β-strand94-103101
β-strand109-118101
β-strand121-12661
β-strand133-13531
α-helix138-15013
α-helix152-16110
α-helix163-17412
β-strand18312
α-helix184-1852
β-strand186-19273
β-strand198-208113
β-strand20912
β-strand214-21854
β-strand22314
β-strand23013
β-strand234-23523
β-strand241-250103
β-strand258-26254
β-strand272-27324
Chain B: 0 helices, 11 β-strands
ElementResiduesLengthSheet
β-strand315
β-strand6-1166
β-strand21-30106
β-strand3115
β-strand36-4167
β-strand44-4527
β-strand50-5126
β-strand55-5626
β-strand62-7096
β-strand78-8367
β-strand91-9447
Chain D: 10 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix14-2411
α-helix27-3610
α-helix50-578
α-helix60-689
α-helix83-908
α-helix93-10210
α-helix116-1238
α-helix126-1349
α-helix149-1568
α-helix159-16810

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
MHC class I antigenAprotein291Homo sapiensQ8WLS4 (AlphaFold model)
Beta-2-microglobulinBprotein100Homo sapiensP61769 (AlphaFold model)
Cancer/testis antigen 1Cprotein9Homo sapiensP78358 (AlphaFold model)
DARPin NY_1Dprotein175synthetic construct
Sequence of entity 1 (A), FASTA
>9FE1_1 MHC class I antigen (chains A)
MGSHSMRYFFTSVSRPGRGEPRFIAVGYVDDTQFVRFDSDAASQRMEPRAPWIEQEGPEY
WDGETRKVKAHSQTHRVDLGTLRGYYNQSEAGSHTVQRMYGCDVGSDWRFLRGYHQYAYD
GKDYIALKEDLRSWTAADMAAQTTKHKWEAAHVAEQLRAYLEGTCVEWLRRYLENGKETL
QRTDAPKTHMTHHAVSDHEATLRCWALSFYPAEITLTWQRDGEDQTQDTELVETRPAGDG
TFQKWAAVVVPSGQEQRYTCHVQHEGLPKPLTLRWEPGSGGSAWSHPQFEK
Sequence of entity 2 (B), FASTA
>9FE1_2 Beta-2-microglobulin (chains B)
MIQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKD
WSFYLLYYTEFTPTEKDEYACRVNHVTLSQPKIVKWDRDM
Sequence of entity 3 (C), FASTA
>9FE1_3 Cancer/testis antigen 1 (chains C)
SLLMWITQV
Sequence of entity 4 (D), FASTA
>9FE1_4 DARPin NY_1 (chains D)
MRGSHHHHHHENLYFQGSDLGKKLLQAARAGQLDEVRELLKAGADVNAKDLIGVTPLHLA
AFSGHLEIVEVLLKASADVNAKDVSGRTPLHVAAKHGHLEIVEVLLKAGADVNAKDLIGF
TPLHLAAQFGHLEIVEVLLKAGADVNAQDKSGKTPADLAARAGHQDIAEVLQKAA

Primary citation

Development of DARPin T cell engagers for specific targeting of tumor-associated HLA/peptide complexes. Venetz-Arenas, N., Schulte, T., Muller, S. et al. iScience (2025) 28:113926-113926. DOI 10.1016/j.isci.2025.113926 · PubMed

Other PDB entries of the same protein (UniProt Q8WLS4 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

About this viewer

MolViewer shows 9FE1 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.