Research workbench
Structure of camp-dependent protein kinase, alpha-catalytic subunit in complex with H8 protein kinase inhibitor [N-(2-METHYLAMINO)ETHYL]-5- isoquinolinesulfonamide
Analyse Structure of camp-dependent protein kinase, alpha-catalytic subunit in complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1YDS
- Type
- protein
- Length
- 356 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- C-AMP-dependent protein kinase; Protein kinase inhibitor peptide
- EC
- 2.7.1.37
- UniProt
- P00517, P04541
- Ligands
- IQS
- Pockets
- 6 · best druggability 0.81
Structure
x-ray diffraction · 2 distinct chains · 37% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| E | C-AMP-dependent protein kinase (EC 2.7.1.37) | protein | 336 | 37% helix, 16% strand | P00517 |
| I | Protein kinase inhibitor peptide | protein | 20 | 30% helix, 0% strand | P04541 |
Ligands and binding sites
- IQS · N-[2-(methylamino)ethyl]-5-isoquinolinesulfonamide · ligand · chains E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 423 | 0.81 | 0.89 | 42 | IQS |
| 2 | 96 | 0.46 | 0.80 | 18 | empty |
| 3 | 63 | 0.41 | 0.80 | 11 | empty |
| 4 | 53 | 0.31 | 0.76 | 13 | empty |
| 5 | 56 | 0.31 | 0.76 | 13 | empty |
Interfaces
1 interface between chains.
- E–I · 1040 Ų buried · 14 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (phosphorylation).
Compared structures
- 1YDS · Structure of CAMP-dependent protein kinase, alpha-catalytic subunit in complex with H8… · the same entry in another collection · chain E against E, 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 P00517
- Every structure of UniProt P04541
- Elsewhere: RCSB PDB 1YDS · PDBe 1YDS · UniProt P00517 · UniProt P04541
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