3O9T: Effector domain from influenza A/PR/8/34 NS1

Effector domain from influenza A/PR/8/34 NS1. Determined by X-ray diffraction at 2.2 Å resolution. Released 11 May 2011.

Method
X-ray diffraction
Resolution
2.2 Å
Organism
Influenza A virus
Chains
2
Atoms
2,011
Mol. weight
34.26 kDa
Released
11 May 2011

Explore 3O9T in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3O9T contains 6 α-helices and 15 β-strands across 2 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: 3 helices, 7 β-strands

ElementResiduesLengthSheet
β-strand88-9141
α-helix95-995
β-strand107-11261
β-strand115-12061
β-strand127-137111
β-strand140-151121
β-strand156-16271
α-helix171-18717
β-strand191-19441
α-helix196-2016
Chain B: 3 helices, 8 β-strands
ElementResiduesLengthSheet
β-strand8511
β-strand88-9142
α-helix95-995
β-strand107-11262
β-strand115-12062
β-strand127-136102
β-strand141-151112
β-strand156-16272
α-helix171-18616
β-strand191-19442
α-helix196-2016

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Nonstructural protein 1A, Bprotein152Influenza A virusP03496 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>3O9T_1 Nonstructural protein 1 (chains A, B)
MTMASVPASRYLTDMTLEEMSRDWSMLIPKQKVAGPLCIRMDQAIMDKNIILKANFSVIF
DRLETLILLRAFTEEGAIVGEISPLPSLPGHTAEDVKNAVGVLIGGLEWNDNTVRVSETL
QRFAWRSSNENGRPPLTPKQKREMAGTIRSEV

Primary citation

A Transient Homotypic Interaction Model for the Influenza A Virus NS1 Protein Effector Domain. Kerry, P.S., Ayllon, J., Taylor, M.A. et al. PLoS One (2011) 6:e17946-e17946. DOI 10.1371/journal.pone.0017946 · PubMed

Other PDB entries of the same protein (UniProt P03496 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

About this viewer

MolViewer shows 3O9T 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.