Research workbench
Structure of the BSK8 kinase domain (semet labeled)
Analyse Structure of the BSK8 kinase domain (semet labeled) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4I93
- Type
- protein
- Length
- 572 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Probable SERINE/THREONINE-protein kinase AT5G41260
- EC
- 2.7.11.1
- UniProt
- Q9FHD7
- Pockets
- 6 · best druggability 0.82
Structure
x-ray diffraction · 2 distinct chains · 45% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Probable SERINE/THREONINE-protein kinase AT5G41260 (EC 2.7.11.1) | protein | 289 | 46% helix, 12% strand | Q9FHD7 |
| B | Probable SERINE/THREONINE-protein kinase AT5G41260 (EC 2.7.11.1) | protein | 283 | 44% helix, 12% strand | Q9FHD7 |
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1101 | 0.82 | 0.83 | 102 | empty |
| 2 | 110 | 0.64 | 0.88 | 21 | empty |
| 3 | 173 | 0.63 | 0.85 | 42 | empty |
| 4 | 73 | 0.39 | 0.79 | 17 | empty |
| 5 | 58 | 0.37 | 0.79 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 538 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 16 modified (engineered).
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 Q9FHD7
- Elsewhere: RCSB PDB 4I93 · PDBe 4I93 · UniProt Q9FHD7
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.