Research workbench
FLRT3 lrr domain
Analyse FLRT3 lrr domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4V2E
- Type
- protein
- Length
- 642 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fibronectin leucine rich transmembrane protein 3
- UniProt
- Q8BGT1
- Pockets
- 2 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 5% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Fibronectin leucine rich transmembrane protein 3 | protein | 321 | 5% helix, 18% strand | Q8BGT1 |
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 | 897 | 0.76 | 0.80 | 72 | empty |
| 2 | 338 | 0.55 | 0.75 | 34 | empty |
Interfaces
1 interface between chains.
- A–B · 1329 Ų buried · 21 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide (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 Q8BGT1
- Elsewhere: RCSB PDB 4V2E · PDBe 4V2E · UniProt Q8BGT1
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.