Research workbench
Crystal structure of the arabidopsis receptor kinase haesa lrr ectdomain in complex with the peptide hormone IDL1.
Analyse Crystal structure of the arabidopsis receptor kinase haesa lrr ectdomain in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5IYV
- Type
- protein
- Length
- 600 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Receptor-like protein kinase 5; Protein ida-like 1
- EC
- 2.7.10.1, 2.7.11.1
- UniProt
- P47735, Q29PV4
- Ligands
- NAG, BMA, MAN
Structure
x-ray diffraction · 2 distinct chains · 19% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Receptor-like protein kinase 5 (EC 2.7.10.1, 2.7.11.1) | protein | 588 | 19% helix, 24% strand | P47735 |
| B | Protein ida-like 1 | protein | 12 | 0% helix, 0% strand | Q29PV4 |
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
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