MolNFT v1 · #20504 · protein

Regulatory subunit of camp dependent protein kinase

1RGS: “Regulatory subunit of camp dependent protein kinase”. X-ray diffraction, 1 ligand (CMP), 3 pockets (best druggability 0.63). MolNFT v1 #20504 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1RGS
Type: protein
Length: 264 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Camp dependent protein kinase
EC: 2.7.1.37
UniProt: P00514
Ligands: CMP
Pockets: 3 · best druggability 0.63

Structure

x-ray diffraction · 1 distinct chain · 35% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Camp dependent protein kinase (EC 2.7.1.37)	protein	264	35% helix, 27% strand	P00514

Ligands and binding sites

CMP · Adenosine-3',5'-cyclic-monophosphate · ligand · 2 copies · chains A

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

Pockets

3 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	175	0.63	0.84	41	empty
2	196	0.62	0.82	29	CMP
3	110	0.60	0.86	21	CMP

Compared structures

1RGS · Regulatory subunit of camp dependent protein kinase · the same entry in another collection · chain A against A, TM-score 1.00
P00514 · AlphaFold monomer V2.0 prediction for camp-dependent protein kinase type I-alpha… · a predicted model of the same protein · chain A against A, TM-score 0.46

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 P00514
Elsewhere: RCSB PDB 1RGS · PDBe 1RGS · UniProt P00514

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