Research workbench
Camp-dependent protein kinase a from cricetulus griseus in complex with fragment like molecule O-guanidino-L-homoserine
Analyse Camp-dependent protein kinase a from cricetulus griseus in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5N3K
- Type
- protein
- Length
- 340 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Camp-dependent protein kinase catalytic subunit alpha
- EC
- 2.7.11.11
- UniProt
- P25321
- Ligands
- GGB
- Pockets
- 4 · best druggability 0.68
Structure
x-ray diffraction · 1 distinct chain · 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 | 340 | 38% helix, 15% strand | P25321 |
Ligands and binding sites
- GGB · L-canavanine · ligand · chains A
- DMS · Dimethyl sulfoxide · additive · 3 copies · chains A
- MPD · (4S)-2-methyl-2,4-pentanediol · additive · 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 379 | 0.68 | 0.81 | 39 | empty |
| 2 | 124 | 0.49 | 0.79 | 16 | MPD |
| 3 | 70 | 0.33 | 0.76 | 19 | empty |
| 4 | 54 | 0.26 | 0.73 | 15 | empty |
Modifications
Observed in the structure: 3 modified (phosphorylation).
Compared structures
- 5N3K · cAMP-dependent Protein Kinase A from Cricetulus griseus in complex with fragment like… · the same entry in another collection · chain A against A, 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 5N3K · PDBe 5N3K · UniProt P25321
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.