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Nvs-PI3-4 bound to the PI3KG catalytic subunit P110 gamma

Analyse Nvs-PI3-4 bound to the PI3KG catalytic subunit P110 gamma in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7JX0
Type: protein
Length: 801 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: VLV
Pockets: 15 · best druggability 0.84

Structure

x-ray diffraction · 1 distinct chain · 48% 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	801	48% helix, 17% strand	P48736

Ligands and binding sites

VLV · N~3~-{[5-(4-acetylphenyl)-4-methyl-1,3-thiazol-2-yl]carbamoyl}-N-tert-butyl-beta-alaninamide · ligand · chains A

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

Pockets

15 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	1032	0.84	0.84	72	empty
2	447	0.69	0.80	43	empty
3	53	0.66	0.96	21	empty
4	220	0.63	0.82	26	VLV
5	154	0.60	0.84	24	empty

Compared structures

7JX0 · NVS-PI3-4 bound to the PI3Kg catalytic subunit p110 gamma · 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 7JX0 · PDBe 7JX0 · UniProt P48736

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