Research workbench

Selective activation of EPAC1 and EPAC2

Analyse Selective activation of EPAC1 and EPAC2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4MGK
Type: protein
Length: 777 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Rap guanine nucleotide exchange factor 4; RAS-related protein rap-1B
UniProt: Q9EQZ6, P61224
Ligands: CMP, SO4
Pockets: 12 · best druggability 0.78

Structure

x-ray diffraction · 2 distinct chains · 48% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
E	Rap guanine nucleotide exchange factor 4	protein	627	52% helix, 15% strand	Q9EQZ6
R	RAS-related protein rap-1B	protein	150	31% helix, 20% strand	P61224

Ligands and binding sites

CMP · Adenosine-3',5'-cyclic-monophosphate · ligand · chains E
SO4 · Sulfate ion · ion · chains R

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

Pockets

12 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1063	0.78	0.80	86	SO4
2	270	0.71	0.85	39	CMP
3	118	0.68	0.90	22	empty
4	138	0.52	0.80	32	empty
5	231	0.49	0.74	33	empty

Interfaces

1 interface between chains.

E–R · 1667 Å² buried · 12 hydrogen bonds · protein-protein

Compared structures

4MGK · Selective activation of Epac1 and Epac2 · the same entry in another collection · chain E against E, TM-score 1.00
P61224 · AlphaFold monomer V2.0 prediction for RAS-related protein rap-1B (P61224) · a predicted model of the same protein · chain R against A, TM-score 0.87
Q9EQZ6 · AlphaFold monomer V2.0 prediction for rap guanine nucleotide exchange factor 4 (Q9EQZ6) · a predicted model of the same protein · chain E against A, TM-score 0.78

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 Q9EQZ6
Every structure of UniProt P61224
Elsewhere: RCSB PDB 4MGK · PDBe 4MGK · UniProt Q9EQZ6 · UniProt P61224

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