Research workbench
Crystal structure of the catalytic subunit of camp-dependent protein kinase complexed with a phosphorylated substrate peptide and detergent
Analyse Crystal structure of the catalytic subunit of camp-dependent protein kinase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1JLU
- Type
- protein
- Length
- 359 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- AMP-dependent protein kinase, alpha-catalytic subunit; Camp-dependent protein kinase…
- EC
- 2.7.1.37
- UniProt
- P05132, P27776
- Pockets
- 4 · best druggability 0.79
Structure
x-ray diffraction · 2 distinct chains · 38% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| E | AMP-dependent protein kinase, alpha-catalytic subunit (EC 2.7.1.37) | protein | 339 | 39% helix, 16% strand | P05132 |
| S | Camp-dependent protein kinase inhibitor, MUSCLE/BRAIN form | protein | 20 | 30% helix, 10% strand | P27776 |
Ligands and binding sites
- OCT · N-octane · additive · chains E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 233 | 0.79 | 0.92 | 37 | empty |
| 2 | 76 | 0.48 | 0.82 | 12 | OCT |
| 3 | 66 | 0.33 | 0.76 | 19 | empty |
| 4 | 53 | 0.29 | 0.76 | 13 | empty |
Interfaces
1 interface between chains.
- E–S · 1077 Ų buried · 19 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 modified (phosphorylation).
Compared structures
- 1JLU · Crystal Structure of the Catalytic Subunit of cAMP-dependent Protein Kinase Complexed… · 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 P05132
- Every structure of UniProt P27776
- Elsewhere: RCSB PDB 1JLU · PDBe 1JLU · UniProt P05132 · UniProt P27776
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