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Co-crystal structure of PKA ri alpha cnb-B mutant (G316R/A336T) with camp

Analyse Co-crystal structure of PKA ri alpha cnb-B mutant (G316R/A336T) with camp in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5KJY
Type: protein
Length: 140 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Camp-dependent protein kinase type I-alpha regulatory subunit
UniProt: P10644
Ligands: CMP
Pockets: 1 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 33% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Camp-dependent protein kinase type I-alpha regulatory subunit	protein	140	37% helix, 33% strand	P10644

Ligands and binding sites

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

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	155	0.69	0.89	27	CMP

Compared structures

5KJY · Co-crystal structure of PKA RI alpha CNB-B mutant (G316R/A336T) with cAMP · the same entry in another collection · chain A against A, TM-score 1.00
P10644 · 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 0.95

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 P10644
Elsewhere: RCSB PDB 5KJY · PDBe 5KJY · UniProt P10644

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