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3-quinoline carboxamides inhibitors of PI3K

Analyse 3-quinoline carboxamides inhibitors of PI3K in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5G55
Type: protein
Length: 847 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit gamma isoform
EC: 2.7.1.137, 2.7.1.153
UniProt: P48736
Ligands: 3QH, SO4
Pockets: 12 · best druggability 0.82

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit gamma isoform (EC 2.7.1.137, 2.7.1.153)	protein	847	43% helix, 17% strand	P48736

Ligands and binding sites

3QH · 6-cyano-4-[[(1R)-1-(4-methylphenyl)ethyl]amino]quinoline-3-carboxamide · ligand · chains A
SO4 · Sulfate ion · ion · chains A

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	1181	0.82	0.83	93	empty
2	632	0.72	0.79	53	3QH
3	361	0.64	0.79	39	empty
4	215	0.58	0.80	34	empty
5	144	0.45	0.76	19	empty

Compared structures

5G55 · 3-Quinoline Carboxamides inhibitors of Pi3K · 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 P48736
Elsewhere: RCSB PDB 5G55 · PDBe 5G55 · UniProt P48736

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