MolNFT v1 · #89160 · protein

Low temperature X-ray structure of camp dependent protein kinase a catalytic subunit with low MG2+, ATP and IP20

4DH1 · Camp-dependent protein kinase catalytic subunit alpha: “Low temperature X-ray structure of camp dependent protein kinase a catalytic subunit with low MG2+, ATP and…”. X-ray diffraction, 2 ligands (ATP, MG), 6 pockets (best…

PDB: 4DH1
Type: protein
Length: 356 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: ATP, MG
Pockets: 6 · best druggability 0.81

Structure

x-ray diffraction · 2 distinct chains · 37% 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	336	37% helix, 16% strand	P05132
I	Camp-dependent protein kinase inhibitor alpha	protein	20	30% helix, 0% strand	P63248

Ligands and binding sites

ATP · Adenosine-5'-triphosphate · ligand · chains A, I
MG · Magnesium ion · metal · chains A

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

Pockets

6 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	182	0.81	0.96	36	MG, ATP
2	90	0.42	0.79	19	empty
3	66	0.41	0.79	12	empty
4	78	0.32	0.74	18	empty
5	51	0.31	0.76	14	empty

Interfaces

1 interface between chains.

A–I · 1062 Å² buried · 21 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 modified (phosphorylation).

Compared structures

4DH1 · Low temperature X-ray structure of cAMP dependent Protein Kinase A catalytic subunit with… · the same entry in another collection · chain A against A, 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 0.41

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 4DH1 · PDBe 4DH1 · UniProt P05132 · UniProt P63248

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