Research workbench
Crystal structures of the myristylated catalytic subunit of camp- dependent protein kinase reveal open and closed conformations
Analyse Crystal structures of the myristylated catalytic subunit of camp- dependent… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1CMK
- Type
- protein
- Length
- 370 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Camp-dependent protein kinase catalytic subunit; Camp-dependent protein kinase inhibitor…
- EC
- 2.7.11.11
- UniProt
- P00517, P61925
- Ligands
- MYR, IOD
- Pockets
- 5 · best druggability 0.73
Structure
x-ray diffraction · 2 distinct chains · 38% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| E | Camp-dependent protein kinase catalytic subunit (EC 2.7.11.11) | protein | 350 | 38% helix, 15% strand | P00517 |
| I | Camp-dependent protein kinase inhibitor, alpha form | protein | 20 | 45% helix, 0% strand | P61925 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 727 | 0.73 | 0.79 | 55 | empty |
| 2 | 66 | 0.53 | 0.86 | 14 | MYR |
| 3 | 92 | 0.36 | 0.75 | 19 | empty |
| 4 | 70 | 0.33 | 0.76 | 18 | empty |
| 5 | 81 | 0.33 | 0.74 | 21 | empty |
Interfaces
1 interface between chains.
- E–I · 910 Ų buried · 19 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified, 1 lipid (phosphorylation, myristoylation).
Compared structures
- 1CMK · Crystal structures of the myristylated catalytic subunit of camp-dependent protein kinase… · the same entry in another collection · chain E against E, TM-score 1.00
- P00517 · AlphaFold monomer V2.0 prediction for camp-dependent protein kinase catalytic subunit… · a predicted model of the same protein · chain E against A, TM-score 0.94
- P61925 · AlphaFold monomer V2.0 prediction for camp-dependent protein kinase inhibitor alpha… · a predicted model of the same protein · chain I against A, TM-score 0.30
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 P00517
- Every structure of UniProt P61925
- Elsewhere: RCSB PDB 1CMK · PDBe 1CMK · UniProt P00517 · UniProt P61925
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