Research workbench
Crystal structure of F327A/K285P mutant of camp-dependent protein kinase
Analyse Crystal structure of F327A/K285P mutant 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
- 2QUR
- Type
- protein
- Length
- 360 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Camp-dependent protein kinase, alpha-catalytic subunit; 20-mer fragment from…
- EC
- 2.7.11.11
- UniProt
- P05132, P63248
- Ligands
- ADP
- Pockets
- 4 · best druggability 0.77
Structure
x-ray diffraction · 2 distinct chains · 38% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Camp-dependent protein kinase, alpha-catalytic subunit (EC 2.7.11.11) | protein | 340 | 38% helix, 15% strand | P05132 |
| B | 20-mer fragment from camp-dependent protein kinase inhibitor alpha | protein | 20 | 35% helix, 5% strand | P63248 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · chains A, B
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 | 849 | 0.77 | 0.81 | 69 | ADP |
| 2 | 169 | 0.50 | 0.77 | 26 | empty |
| 3 | 74 | 0.33 | 0.76 | 17 | empty |
| 4 | 63 | 0.28 | 0.73 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 894 Ų buried · 16 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (phosphorylation).
Compared structures
- 2QUR · Crystal Structure of F327A/K285P Mutant of cAMP-dependent Protein Kinase · the same entry in another collection · chain A against A, TM-score 1.00
- P63248 · AlphaFold monomer V2.0 prediction for camp-dependent protein kinase inhibitor alpha… · a predicted model of the same protein · chain B against A, TM-score 0.36
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 P63248
- Elsewhere: RCSB PDB 2QUR · PDBe 2QUR · UniProt P05132 · UniProt P63248
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