Research workbench
Structure of the bovine P85A bh domain
Analyse Structure of the bovine P85A bh domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6D82
- Type
- protein
- Length
- 358 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphatidylinositol 3-kinase regulatory subunit alpha
- UniProt
- P23727
- Ligands
- SO4
- Pockets
- 2 · best druggability 0.46
Structure
x-ray diffraction · 2 distinct chains · 63% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | Phosphatidylinositol 3-kinase regulatory subunit alpha | protein | 176 | 63% helix, 0% strand | P23727 |
| A | Phosphatidylinositol 3-kinase regulatory subunit alpha | protein | 182 | 62% helix, 0% strand | P23727 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 3 copies · chains B, A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 144 | 0.46 | 0.76 | 25 | empty |
| 2 | 60 | 0.39 | 0.80 | 11 | empty |
Interfaces
1 interface between chains.
- B–A · 387 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (oxidation).
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 P23727
- Elsewhere: RCSB PDB 6D82 · PDBe 6D82 · UniProt P23727
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.