Research workbench
Crystal structure of type iia holoenzyme of camp-dependent protein kinase
Analyse Crystal structure of type iia holoenzyme 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
- 2QVS
- Type
- protein
- Length
- 623 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Camp-dependent protein kinase, alpha-catalytic subunit; Camp-dependent protein kinase…
- EC
- 2.7.11.11
- UniProt
- P05132, P12367
- Pockets
- 10 · best druggability 0.69
Structure
x-ray diffraction · 2 distinct chains · 35% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| E | Camp-dependent protein kinase, alpha-catalytic subunit (EC 2.7.11.11) | protein | 325 | 37% helix, 13% strand | P05132 |
| B | Camp-dependent protein kinase type II-alpha regulatory subunit | protein | 298 | 33% helix, 32% strand | P12367 |
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 | 738 | 0.69 | 0.76 | 68 | empty |
| 2 | 270 | 0.59 | 0.79 | 39 | empty |
| 3 | 274 | 0.58 | 0.78 | 36 | empty |
| 4 | 209 | 0.58 | 0.80 | 32 | empty |
| 5 | 275 | 0.57 | 0.78 | 38 | empty |
Interfaces
1 interface between chains.
- E–B · 1818 Ų buried · 37 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (phosphorylation).
Compared structures
- 2QVS · Crystal Structure of Type IIa Holoenzyme of cAMP-dependent Protein Kinase · the same entry in another collection · chain E against E, TM-score 1.00
- P12367 · AlphaFold monomer V2.0 prediction for camp-dependent protein kinase type II-alpha… · a predicted model of the same protein · chain B against A, TM-score 0.97
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 P12367
- Elsewhere: RCSB PDB 2QVS · PDBe 2QVS · UniProt P05132 · UniProt P12367
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