MolNFT v1 · #147739 · protein
Crystal structure of the protein-kinase a catalytic subunit from criteculus griseus in complex with compounds RKP182 and RKP117
6EMD · Camp-dependent protein kinase catalytic subunit alpha: “Crystal structure of the protein-kinase a catalytic subunit from criteculus griseus in complex with compounds…”. X-ray diffraction, 1 ligand (9LQ), 4 pockets (best druggability…
- PDB
- 6EMD
- Type
- protein
- Length
- 361 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
- P25321
- Ligands
- 9LQ
- Pockets
- 4 · best druggability 0.78
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 | 343 | 39% helix, 15% strand | P25321 |
| D | Camp-dependent protein kinase inhibitor | protein | 18 | 28% helix, 0% strand | — |
Ligands and binding sites
- 9LQ · [2-[(4-isoquinolin-5-ylsulfonyl-1,4-diazepan-1-yl) methyl]phenyl]boronic acid · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 565 | 0.78 | 0.84 | 45 | 9LQ |
| 2 | 246 | 0.56 | 0.77 | 31 | empty |
| 3 | 52 | 0.33 | 0.78 | 17 | empty |
| 4 | 63 | 0.30 | 0.75 | 19 | empty |
Interfaces
1 interface between chains.
- A–D · 845 Ų buried · 17 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 modified (phosphorylation).
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 P25321
- Elsewhere: RCSB PDB 6EMD · PDBe 6EMD · UniProt P25321
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