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Structure of PI3K gamma in complex with an inhibitor

Analyse Structure of PI3K gamma in complex with an inhibitor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4XX5
Type: protein
Length: 843 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: 43R
Pockets: 14 · best druggability 0.81

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit gamma isoform (EC 2.7.1.153, 2.7.11.1)	protein	843	45% helix, 17% strand	P48736

Ligands and binding sites

43R · N-[5-(5-methoxypyridin-3-yl)-4,5,6,7-tetrahydro[1,3]thiazolo[5,4-c]pyridin-2-yl]acetamide · ligand · chains A

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

Pockets

14 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1170	0.81	0.82	70	empty
2	521	0.73	0.81	53	43R
3	53	0.69	0.98	20	empty
4	517	0.69	0.79	78	empty
5	139	0.60	0.84	19	empty

Compared structures

4XX5 · Structure of PI3K gamma in complex with an inhibitor · 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 4XX5 · PDBe 4XX5 · UniProt P48736

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