Research workbench
AMP-activated protein kinase (ampk) inhibition by sbi-0206965: alpha 2 kinase domain bound to sbi-0206965
Analyse AMP-activated protein kinase (ampk) inhibition by sbi-0206965: alpha 2 kinase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6BX6
- Type
- protein
- Length
- 243 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 5'-AMP-activated protein kinase catalytic subunit alpha-2
- EC
- 2.7.11.1, 2.7.11.27, 2.7.11.31
- UniProt
- P54646
- Ligands
- EDJ
- Pockets
- 2 · best druggability 0.59
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 5'-AMP-activated protein kinase catalytic subunit alpha-2 (EC 2.7.11.1, 2.7.11.27, 2.7.11.31) | protein | 243 | 37% helix, 18% strand | P54646 |
Ligands and binding sites
- EDJ · 2-({5-bromo-2-[(3,4,5-trimethoxyphenyl)amino]pyrimidin-4-yl}oxy)-N-methylbenzene-1-carboximidic acid · ligand · chains 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 302 | 0.59 | 0.78 | 28 | EDJ |
| 2 | 67 | 0.36 | 0.77 | 19 | empty |
Compared structures
- 6BX6 · AMP-Activated protein kinase (AMPK) inhibition by SBI-0206965: alpha 2 kinase domain… · the same entry in another collection · chain A against A, TM-score 1.00
- P54646 · AlphaFold monomer V2.0 prediction for 5'-AMP-activated protein kinase catalytic subunit… · a predicted model of the same protein · chain A against A, TM-score 0.91
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 P54646
- Elsewhere: RCSB PDB 6BX6 · PDBe 6BX6 · UniProt P54646
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