Research workbench
Crystal structure of E230Q mutant of camp-dependent protein kinase reveals unexpected apoenzyme conformation
Analyse Crystal structure of E230Q mutant of camp-dependent protein kinase reveals… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1SYK
- Type
- protein
- Length
- 675 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Camp-dependent protein kinase, alpha-catalytic subunit
- EC
- 2.7.1.37
- UniProt
- P05132
- Pockets
- 8 · best druggability 0.70
Structure
x-ray diffraction · 2 distinct chains · 40% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Camp-dependent protein kinase, alpha-catalytic subunit (EC 2.7.1.37) | protein | 350 | 40% helix, 15% strand | P05132 |
| B | Camp-dependent protein kinase, alpha-catalytic subunit (EC 2.7.1.37) | protein | 325 | 39% helix, 16% strand | P05132 |
Pockets
8 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 662 | 0.70 | 0.78 | 60 | empty |
| 2 | 335 | 0.61 | 0.77 | 37 | empty |
| 3 | 381 | 0.60 | 0.76 | 38 | empty |
| 4 | 248 | 0.53 | 0.76 | 27 | empty |
| 5 | 112 | 0.45 | 0.78 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 714 Ų buried · 11 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 modified (phosphorylation).
Compared structures
- 1SYK · Crystal structure of E230Q mutant of cAMP-dependent protein kinase reveals unexpected… · 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 P05132
- Elsewhere: RCSB PDB 1SYK · PDBe 1SYK · UniProt P05132
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