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Crystal structure of LYK3 ectodomain
Analyse Crystal structure of LYK3 ectodomain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6XWE
- Type
- protein
- Length
- 204 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Lysm domain receptor-like kinase 3
- EC
- 2.7.11.1
- UniProt
- Q6UD73
- Ligands
- CCN, NAG, BMA, FUC
- Pockets
- 1 · best druggability 0.63
Structure
x-ray diffraction · 1 distinct chain · 20% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Lysm domain receptor-like kinase 3 (EC 2.7.11.1) | protein | 204 | 20% helix, 26% strand | Q6UD73 |
Ligands and binding sites
- CCN · Acetonitrile · ligand · chains A
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 5 copies · chains A
- BMA · beta-D-mannopyranose · sugar
- FUC · alpha-L-fucopyranose · sugar · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 256 | 0.63 | 0.81 | 35 | empty |
Modifications
Observed in the structure: 3 disulfide, 3 glycan (disulfide, N-glycosylation).
Compared structures
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 Q6UD73
- Elsewhere: RCSB PDB 6XWE · PDBe 6XWE · UniProt Q6UD73
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