The crystal structure of the arabidopsis receptor kinase haesa lrr ectdomain in complex with a N-terminal extended ida peptide hormone ligand.

Structure

x-ray diffraction · 2 distinct chains · 18% helix, 25% strand (DSSP).

Ligands and binding sites

• NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 11 copies · chains A, B
• BMA · beta-D-mannopyranose · sugar
• MAN · alpha-D-mannopyranose · sugar · chains A
• MG · Magnesium ion · metal · 2 copies · chains A
• EDO · 1,2-ethanediol · additive · chains B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Interfaces

1 interface between chains.

• A–B · 770 Ų buried · 16 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 7 glycan, 4 disulfide, 1 modified (N-glycosylation, disulfide, hydroxylation).

Compared structures

• 5IXT · The crystal structure of the Arabidopsis receptor kinase HAESA LRR ectdomain in complex… · the same entry in another collection · chain A against A, TM-score 1.00
• P47735 · AlphaFold monomer V2.0 prediction for receptor-like protein kinase 5 (P47735) · a predicted model of the same protein · chain A against A, TM-score 0.98
• Q8LAD7 · AlphaFold monomer V2.0 prediction for protein ida (Q8LAD7) · a predicted model of the same protein · chain B against A, TM-score 0.29

Analyse

• Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
• Every structure of UniProt P47735
• Every structure of UniProt Q8LAD7
• Elsewhere: RCSB PDB 5IXT · PDBe 5IXT · UniProt P47735 · UniProt Q8LAD7