Research workbench
Crystal structure of a tdr receptor
Analyse Crystal structure of a tdr receptor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5JFK
- Type
- protein
- Length
- 1,154 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Leucine-rich repeat receptor-like protein kinase tdr
- EC
- 2.7.11.1
- UniProt
- Q9FII5
- Ligands
- NAG
- Pockets
- 2 · best druggability 0.59
Structure
x-ray diffraction · 1 distinct chain · 15% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Leucine-rich repeat receptor-like protein kinase tdr (EC 2.7.11.1) | protein | 577 | 15% helix, 21% strand | Q9FII5 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 10 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 97 | 0.59 | 0.87 | 27 | empty |
| 2 | 92 | 0.56 | 0.85 | 26 | empty |
Modifications
Observed in the structure: 10 glycan, 4 disulfide (N-glycosylation, disulfide).
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 Q9FII5
- Elsewhere: RCSB PDB 5JFK · PDBe 5JFK · UniProt Q9FII5
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