MolNFT v1 · #147561 · protein
Crystal structure of the protein-kinase a catalytic subunit from criteculus griseus in complex with compounds RKP120 and RKP190
6EH3 · 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 (B4Z), 3 pockets (best druggability…
- PDB
- 6EH3
- Type
- protein
- Length
- 371 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
- B4Z
- Pockets
- 3 · best druggability 0.77
Structure
x-ray diffraction · 2 distinct chains · 39% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Camp-dependent protein kinase catalytic subunit alpha (EC 2.7.11.11) | protein | 353 | 39% helix, 15% strand | P25321 |
| C | Camp-dependent protein kinase inhibitor | protein | 18 | 44% helix, 0% strand | — |
Ligands and binding sites
- B4Z · ~{N}-[2-[(phenylmethyl)amino]ethyl]isoquinoline-5-sulfonamide · ligand · chains A, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 507 | 0.77 | 0.85 | 48 | B4Z |
| 2 | 226 | 0.59 | 0.80 | 33 | empty |
| 3 | 67 | 0.28 | 0.72 | 22 | empty |
Interfaces
1 interface between chains.
- A–C · 824 Ų buried · 17 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 modified (phosphorylation).
Compared structures
- 6EH3 · Crystal Structure of the Protein-Kinase A catalytic subunit from Criteculus Griseus in… · the same entry in another collection · chain C against C, TM-score 1.00
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 6EH3 · PDBe 6EH3 · UniProt P25321
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.