Research workbench
Regulatory subunit of a cAMP-independent protein kinase A from Trypanosoma brucei at 2.1 Angstrom resolution
Analyse Regulatory subunit of a cAMP-independent protein kinase A from Trypanosoma… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6FLO
- Type
- protein
- Length
- 549 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.13869
- Source
- Trypanosoma brucei brucei TREU927
- Molecule
- Protein kinase A regulatory subunit
- UniProt
- Q385V6
- Ligands
- NOS
- Pockets
- 10 · best druggability 0.76
Structure
x-ray diffraction · resolution 2.13869 · 2 distinct chains · 37% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein kinase A regulatory subunit | protein | 277 | 37% helix, 29% strand | Q385V6 |
| B | Protein kinase A regulatory subunit | protein | 272 | 36% helix, 30% strand | Q385V6 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 91 | 0.76 | 0.97 | 20 | NOS |
| 2 | 96 | 0.76 | 0.96 | 21 | NOS |
| 3 | 293 | 0.60 | 0.78 | 46 | NOS |
| 4 | 106 | 0.59 | 0.86 | 23 | NOS |
| 5 | 284 | 0.53 | 0.75 | 29 | empty |
Interfaces
1 interface between chains.
- A–B · 696 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
- 6FLO · Regulatory subunit of a camp-independent protein kinase a from trypanosoma brucei at 2.1… · the same entry in another collection · chain A against A, TM-score 1.00
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 Q385V6
- Elsewhere: RCSB PDB 6FLO · PDBe 6FLO · UniProt Q385V6
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