Research workbench
Human camp dependent protein kinase in complex with phenol
Analyse Human camp dependent protein kinase in complex with phenol in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3NX8
- Type
- protein
- Length
- 354 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Camp-dependent protein kinase catalytic subunit alpha; Camp-dependent protein kinase…
- EC
- 2.7.11.11
- UniProt
- P17612, P61925
- Ligands
- IPH
- Pockets
- 3 · best druggability 0.75
Structure
x-ray diffraction · 2 distinct chains · 38% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Camp-dependent protein kinase catalytic subunit alpha (EC 2.7.11.11) | protein | 336 | 38% helix, 15% strand | P17612 |
| B | Camp-dependent protein kinase inhibitor alpha | protein | 18 | 39% helix, 0% strand | P61925 |
Ligands and binding sites
- IPH · Phenol · ligand · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 86 | 0.75 | 0.97 | 25 | IPH |
| 2 | 106 | 0.43 | 0.77 | 21 | empty |
| 3 | 83 | 0.33 | 0.74 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 907 Ų buried · 22 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 modified (phosphorylation, nonstandard).
Compared structures
- 3NX8 · human cAMP dependent protein kinase in complex with phenol · the same entry in another collection · chain A against A, TM-score 1.00
- P17612 · 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 P17612
- Every structure of UniProt P61925
- Elsewhere: RCSB PDB 3NX8 · PDBe 3NX8 · UniProt P17612 · UniProt P61925
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