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
- 4JYO
- Type
- protein
- Length
- 217 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Angiopoietin-1
- UniProt
- Q15389
- Ligands
- CA
- Pockets
- 1 · best druggability 0.36
Structure
x-ray diffraction · 1 distinct chain · 13% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| X | Angiopoietin-1 | protein | 217 | 13% helix, 31% strand | Q15389 |
Ligands and binding sites
- CA · Calcium ion · metal · chains X
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 71 | 0.36 | 0.77 | 18 | empty |
Modifications
Observed in the structure: 3 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 Q15389
- Elsewhere: RCSB PDB 4JYO · PDBe 4JYO · UniProt Q15389
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