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Crystal structure of myristoylated K7C catalytic subunit of camp- dependent protein kinase in complex with SP20

Analyse Crystal structure of myristoylated K7C 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: 4DFZ
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 alpha; Camp-dependent protein kinase…
EC: 2.7.11.11
UniProt: P05132, P63248
Ligands: MYR
Pockets: 4 · best druggability 0.81

Structure

x-ray diffraction · 2 distinct chains · 37% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
E	Camp-dependent protein kinase catalytic subunit alpha (EC 2.7.11.11)	protein	350	37% helix, 15% strand	P05132
I	Camp-dependent protein kinase inhibitor alpha	protein	20	30% helix, 10% strand	P63248

Ligands and binding sites

MYR · Myristic acid · ligand · chains E

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.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	333	0.81	0.90	43	empty
2	209	0.56	0.79	26	MYR
3	83	0.37	0.76	15	empty
4	87	0.33	0.74	15	empty

Interfaces

1 interface between chains.

E–I · 1018 Å² buried · 23 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 modified, 1 lipid (phosphorylation, myristoylation).

Compared structures

4DFZ · Crystal structure of myristoylated K7C catalytic subunit of cAMP-dependent protein kinase… · the same entry in another collection · chain E against E, TM-score 1.00
P63248 · 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 0.40

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 P05132
Every structure of UniProt P63248
Elsewhere: RCSB PDB 4DFZ · PDBe 4DFZ · UniProt P05132 · UniProt P63248

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