MolNFT v1 · #148793 · protein

PI3KG in complex with compound 7

6FH5 · Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic…: “PI3KG in complex with compound 7”. X-ray diffraction, 1 ligand (DD8), 12 pockets (best druggability 0.83). MolNFT v1 #148793 on GenesisL1: 3D structure, binding sites and…

PDB: 6FH5
Type: protein
Length: 802 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: 2.7.1.153, 2.7.11.1
UniProt: P48736
Ligands: DD8
Pockets: 12 · best druggability 0.83

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit gamma isoform (EC 2.7.1.153, 2.7.11.1)	protein	802	45% helix, 18% strand	P48736

Ligands and binding sites

DD8 · 3-methyl-1-(oxan-4-yl)-8-pyridin-3-yl-imidazo[4,5-c]quinolin-2-one · ligand · 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, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1042	0.83	0.84	82	empty
2	369	0.70	0.82	39	DD8
3	417	0.65	0.78	42	empty
4	303	0.61	0.79	48	empty
5	74	0.55	0.86	20	empty

Compared structures

6FH5 · PI3Kg IN COMPLEX WITH Compound 7 · 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 6FH5 · PDBe 6FH5 · UniProt P48736

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