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Crystal structure of the catalytic subunit of camp-dependent protein kinase complexed with a substrate peptide, ADP and detergent

Analyse Crystal structure of the catalytic subunit of camp-dependent protein kinase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1JBP
Type: protein
Length: 362 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Camp-dependent protein kinase, alpha-catalytic subunit; Camp-dependent protein kinase…
EC: 2.7.1.37
UniProt: P05132, P27776
Ligands: ADP
Pockets: 6 · best druggability 0.80

Structure

x-ray diffraction · 2 distinct chains · 38% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
E	Camp-dependent protein kinase, alpha-catalytic subunit (EC 2.7.1.37)	protein	342	38% helix, 16% strand	P05132
S	Camp-dependent protein kinase inhibitor, MUSCLE/BRAIN form	protein	20	30% helix, 10% strand	P27776

Ligands and binding sites

ADP · Adenosine-5'-diphosphate · ligand · chains E, S
OCT · N-octane · additive · chains E

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

6 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	223	0.80	0.93	39	ADP
2	135	0.51	0.79	18	OCT
3	51	0.34	0.79	18	empty
4	67	0.33	0.76	20	empty
5	76	0.30	0.73	17	empty

Interfaces

1 interface between chains.

E–S · 1054 Å² buried · 24 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 modified (phosphorylation).

Compared structures

1JBP · Crystal Structure of the Catalytic Subunit of cAMP-dependent Protein Kinase Complexed… · the same entry in another collection · chain E against E, TM-score 1.00
P05132 · 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 0.99

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 P27776
Elsewhere: RCSB PDB 1JBP · PDBe 1JBP · UniProt P05132 · UniProt P27776

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