Research workbench
Crystal structure of ANXUR2 extracellular domain from arabidopsis thaliana
Analyse Crystal structure of ANXUR2 extracellular domain from arabidopsis thaliana in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5Y92
- Type
- protein
- Length
- 387 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Receptor-like protein kinase ANXUR2
- EC
- 2.7.11.1
- UniProt
- Q3E8W4
- Ligands
- NAG, BMA
- Pockets
- 3 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 9% helix, 40% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Receptor-like protein kinase ANXUR2 (EC 2.7.11.1) | protein | 387 | 9% helix, 40% strand | Q3E8W4 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 7 copies · chains A
- BMA · beta-D-mannopyranose · sugar · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 634 | 0.78 | 0.83 | 65 | empty |
| 2 | 70 | 0.46 | 0.83 | 16 | empty |
| 3 | 60 | 0.26 | 0.73 | 19 | empty |
Modifications
Observed in the structure: 4 glycan (N-glycosylation).
Compared structures
- 5Y92 · Crystal structure of ANXUR2 extracellular domain from Arabidopsis thaliana · the same entry in another collection · chain A against A, TM-score 1.00
- Q3E8W4 · AlphaFold monomer V2.0 prediction for receptor-like protein kinase ANXUR2 (Q3E8W4) · a predicted model of the same protein · chain A against A, TM-score 1.00
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 Q3E8W4
- Elsewhere: RCSB PDB 5Y92 · PDBe 5Y92 · UniProt Q3E8W4
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