Research workbench
Structural basis for angiopoietin-1 mediated signaling initiation
Analyse Structural basis for angiopoietin-1 mediated signaling initiation in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4K0V
- Type
- protein
- Length
- 731 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tek tyrosine kinase variant; Angiopoietin-1
- UniProt
- Q59HG2, Q15389
- Pockets
- 10 · best druggability 0.71
Structure
x-ray diffraction · 2 distinct chains · 5% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tek tyrosine kinase variant | protein | 514 | 1% helix, 36% strand | Q59HG2 |
| B | Angiopoietin-1 | protein | 217 | 12% helix, 31% strand | Q15389 |
Pockets
10 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 381 | 0.71 | 0.83 | 47 | empty |
| 2 | 521 | 0.70 | 0.79 | 59 | empty |
| 3 | 166 | 0.55 | 0.80 | 20 | empty |
| 4 | 175 | 0.51 | 0.78 | 30 | empty |
| 5 | 85 | 0.43 | 0.78 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 615 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 17 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 Q59HG2
- Every structure of UniProt Q15389
- Elsewhere: RCSB PDB 4K0V · PDBe 4K0V · UniProt Q59HG2 · UniProt Q15389
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.