MolNFT v1 · #134371 · protein

PI3KG in complex with 5D

5T23 · Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic…: “PI3KG in complex with 5D”. X-ray diffraction, 1 ligand (74F), 17 pockets (best druggability 0.82). MolNFT v1 #134371 on GenesisL1: 3D structure, binding sites and pockets…

PDB: 5T23
Type: protein
Length: 804 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: 74F
Pockets: 17 · best druggability 0.82

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	804	45% helix, 18% strand	P48736

Ligands and binding sites

74F · 3-(benzotriazol-1-yl)-5-[1-methyl-5-[(1~{S})-1-morpholin-4-ylethyl]-1,2,4-triazol-3-yl]pyrazin-2-amine · ligand · chains A

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

Pockets

17 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1170	0.82	0.83	72	empty
2	531	0.68	0.78	58	empty
3	304	0.65	0.81	35	74F
4	56	0.64	0.94	15	empty
5	184	0.58	0.81	32	empty

Compared structures

5T23 · PI3Kg IN COMPLEX WITH 5d · 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 5T23 · PDBe 5T23 · UniProt P48736

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