MolNFT v1 · #30661 · protein

Crystal structure of human PI3KGAMMA complexed with AS605240

2A5U · Phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic…: “Crystal structure of human PI3KGAMMA complexed with AS605240”. X-ray diffraction, 1 ligand (QYT), 14 pockets (best druggability 0.83). MolNFT v1 #30661 on GenesisL1: 3D…

PDB: 2A5U
Type: protein
Length: 839 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
UniProt: P48736
Ligands: QYT
Pockets: 14 · best druggability 0.83

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 16% 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)	protein	839	42% helix, 16% strand	P48736

Ligands and binding sites

QYT · (5E)-5-(quinoxalin-6-ylmethylene)-1,3-thiazolidine-2,4-dione · 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, 8 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1034	0.83	0.83	75	empty
2	432	0.70	0.81	51	empty
3	51	0.67	0.97	21	empty
4	407	0.66	0.79	42	QYT
5	310	0.58	0.77	32	empty

Compared structures

2A5U · Crystal Structure of human PI3Kgamma complexed with AS605240 · 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 2A5U · PDBe 2A5U · UniProt P48736

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