MolNFT v1 · #101517 · protein

Apo structure of the catalytic subunit of camp-dependent protein kinase

4NTS · Camp-dependent protein kinase catalytic subunit alpha: “Apo structure of the catalytic subunit of camp-dependent protein kinase”. X-ray diffraction, 1 ligand (MYR), 6 pockets (best druggability 0.63). MolNFT v1 #101517 on GenesisL1…

PDB: 4NTS
Type: protein
Length: 686 residues
Chains: 2
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: P05132
Ligands: MYR
Pockets: 6 · best druggability 0.63

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Camp-dependent protein kinase catalytic subunit alpha (EC 2.7.11.11)	protein	343	37% helix, 15% strand	P05132

Ligands and binding sites

MYR · Myristic acid · ligand · 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, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	414	0.63	0.77	42	empty
2	346	0.60	0.77	38	empty
3	90	0.50	0.82	12	MYR
4	107	0.45	0.78	14	empty
5	101	0.37	0.75	26	empty

Modifications

Observed in the structure: 4 modified (phosphorylation).

Compared structures

4NTS · Apo structure of the catalytic subunit of cAMP-dependent protein kinase · 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 P05132
Elsewhere: RCSB PDB 4NTS · PDBe 4NTS · UniProt P05132

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