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Discovery of small molecules that bind to K-RAS and inhibit sos- mediated activation

Analyse Discovery of small molecules that bind to K-RAS and inhibit sos- mediated… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4EPX
Type: protein
Length: 170 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: GTPase KRAS
EC: 3.6.5.2
UniProt: P01116
Ligands: GDP, 0QR, MG
Pockets: 2 · best druggability 0.48

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	GTPase KRAS (EC 3.6.5.2)	protein	170	38% helix, 24% strand	P01116

Ligands and binding sites

GDP · Guanosine-5'-diphosphate · ligand · chains A
0QR · N-(6-aminopyridin-2-yl)-4-fluorobenzenesulfonamide · ligand · chains A
MG · Magnesium ion · metal · 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	139	0.48	0.78	26	GDP, MG
2	62	0.35	0.78	19	empty

Compared structures

4EPX · Discovery of Small Molecules that Bind to K-Ras and Inhibit Sos-mediated Activation · 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 P01116
Elsewhere: RCSB PDB 4EPX · PDBe 4EPX · UniProt P01116

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