MolNFT v1 · #2066 · protein
A binary complex of the catalytic subunit of camp-dependent protein kinase and adenosine further defines conformational flexibility
1BKX: “A binary complex of the catalytic subunit of camp-dependent protein kinase and adenosine further defines…”. X-ray diffraction, 1 ligand (A), 5 pockets (best druggability 0.69). MolNFT v1 #2066 on GenesisL1: 3D structure, binding…
- PDB
- 1BKX
- Type
- protein
- Length
- 339 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Camp-dependent protein kinase
- EC
- 2.7.1.37
- UniProt
- P05132
- Ligands
- A
- Pockets
- 5 · best druggability 0.69
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Camp-dependent protein kinase (EC 2.7.1.37) | protein | 339 | 37% helix, 16% strand | P05132 |
Ligands and binding sites
- A · Adenosine-5'-monophosphate · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 264 | 0.69 | 0.84 | 34 | A |
| 2 | 98 | 0.41 | 0.78 | 19 | empty |
| 3 | 111 | 0.38 | 0.75 | 20 | empty |
| 4 | 60 | 0.34 | 0.77 | 14 | empty |
| 5 | 74 | 0.34 | 0.76 | 19 | empty |
Modifications
Observed in the structure: 2 modified (phosphorylation).
Compared structures
- 1BKX · A binary complex of the catalytic subunit of camp-dependent protein kinase and adenosine… · the same entry in another collection · chain A against A, TM-score 1.00
- P05132 · AlphaFold monomer V2.0 prediction for camp-dependent protein kinase catalytic subunit… · a predicted model of the same protein · chain A against A, TM-score 0.99
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 1BKX · PDBe 1BKX · UniProt P05132
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