Research workbench
Crystal structure of the arabidopsis receptor kinase haesa lrr ectdomain (apo form).
Analyse Crystal structure of the arabidopsis receptor kinase haesa lrr ectdomain (apo… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5IXO
- Type
- protein
- Length
- 596 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Receptor-like protein kinase 5
- EC
- 2.7.10.1, 2.7.11.1
- UniProt
- P47735
- Ligands
- NAG, MG
Structure
x-ray diffraction · 1 distinct chain · 18% helix, 26% 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 | 596 | 18% helix, 26% strand | P47735 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 9 copies · chains A
- MG · Magnesium ion · metal · chains A
- EDO · 1,2-ethanediol · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 6 glycan, 4 disulfide (N-glycosylation, disulfide).
Compared structures
- 5IXO · Crystal structure of the Arabidopsis receptor kinase HAESA LRR ectdomain (apo form). · 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
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
- Elsewhere: RCSB PDB 5IXO · PDBe 5IXO · UniProt P47735
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.