Research workbench

Crystal structure of the apo p110alpha catalytic subunit from homo sapiens

Analyse Crystal structure of the apo p110alpha catalytic subunit from homo sapiens in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 8BFU
Type: protein
Length: 880 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.41
Source: Homo sapiens
Molecule: Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform
EC: 2.7.1.137, 2.7.1.153, 2.7.11.1
UniProt: P42336
Pockets: 7 · best druggability 0.84

Structure

x-ray diffraction · resolution 2.41 · 1 distinct chain · 45% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform (EC 2.7.1.137, 2.7.1.153, 2.7.11.1)	protein	880	45% helix, 17% strand	P42336

Pockets

7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	991	0.84	0.85	85	empty
2	1040	0.77	0.79	121	empty
3	389	0.66	0.80	39	empty
4	255	0.58	0.78	36	empty
5	134	0.50	0.79	19	empty

Compared structures

P42336 · AlphaFold monomer V2.0 prediction for phosphatidylinositol 4,5-bisphosphate 3-kinase… · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P42336
Elsewhere: RCSB PDB 8BFU · PDBe 8BFU · UniProt P42336

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.