Research workbench

Crystal structure of BCY1, the yeast regulatory subunit of PKA

Analyse Crystal structure of BCY1, the yeast regulatory subunit of PKA in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3OF1
Type: protein
Length: 246 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Camp-dependent protein kinase regulatory subunit
UniProt: P07278
Ligands: CMP
Pockets: 2 · best druggability 0.60

Structure

x-ray diffraction · 1 distinct chain · 29% helix, 32% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Camp-dependent protein kinase regulatory subunit	protein	246	29% helix, 32% strand	P07278

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

2 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	196	0.60	0.81	29	CMP
2	157	0.57	0.82	22	CMP

Compared structures

3OF1 · Crystal Structure of Bcy1, the Yeast Regulatory Subunit of PKA · the same entry in another collection · chain A against A, TM-score 1.00
P07278 · AlphaFold monomer V2.0 prediction for camp-dependent protein kinase regulatory subunit… · a predicted model of the same protein · chain A against A, TM-score 0.56

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 P07278
Elsewhere: RCSB PDB 3OF1 · PDBe 3OF1 · UniProt P07278

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.