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The crystal structure of truncated mouse BET3P
Analyse The crystal structure of truncated mouse BET3P in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1WC9
- Type
- protein
- Length
- 160 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Trafficking protein particle complex SUBUNIT3
- UniProt
- O55013
- Ligands
- MYR
- Pockets
- 1 · best druggability 0.72
Structure
x-ray diffraction · 1 distinct chain · 48% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Trafficking protein particle complex SUBUNIT3 | protein | 160 | 48% helix, 18% strand | O55013 |
Ligands and binding sites
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 | 296 | 0.72 | 0.85 | 36 | MYR |
Modifications
Observed in the structure: 1 lipid (myristoylation).
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 O55013
- Elsewhere: RCSB PDB 1WC9 · PDBe 1WC9 · UniProt O55013
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