Crystal structure of the arabidopsis receptor kinase haesa lrr ectdomain in complex with the peptide hormone IDL1.

Structure

x-ray diffraction · 2 distinct chains · 19% helix, 24% strand (DSSP).

Ligands and binding sites

• NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 11 copies · chains A
• BMA · beta-D-mannopyranose · sugar
• MAN · alpha-D-mannopyranose · sugar
• 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 · 774 Ų buried · 15 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 7 glycan, 3 disulfide, 1 modified (N-glycosylation, disulfide, hydroxylation).

Compared structures

• 5IYV · Crystal structure of the Arabidopsis receptor kinase HAESA LRR ectdomain in complex with… · 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 0.99
• Q29PV4 · AlphaFold monomer V2.0 prediction for protein ida-like 1 (Q29PV4) · a predicted model of the same protein · chain B against A, TM-score 0.33

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 Q29PV4
• Elsewhere: RCSB PDB 5IYV · PDBe 5IYV · UniProt P47735 · UniProt Q29PV4