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AlphaFold monomer V2.0 prediction for phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform (P42337)

Analyse AlphaFold monomer V2.0 prediction for phosphatidylinositol 4,5-bisphosphate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession: P42337
Type: protein
Length: 1,068 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0xaBbD25c712F347D2D5B94763092EE1754834376F
Molecule: Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform
UniProt: P42337
Pockets: 13 · best druggability 0.85

Structure

1 distinct chain · 42% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform	protein	1068	42% helix, 19% strand	P42337

Pockets

13 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	1083	0.85	0.86	92	empty
2	817	0.74	0.79	71	empty
3	632	0.70	0.78	54	empty
4	516	0.68	0.78	66	empty
5	236	0.65	0.83	35	empty

Compared structures

4A55 · Crystal structure of p110alpha in complex with iSH2 of p85alpha and the inhibitor PIK-108 · an experimental structure of the same protein · chain A against A, TM-score 0.92
4A55 · Crystal structure of P110ALPHA in complex with ISH2 of P85ALPHA and the inhibitor pik-108 · an experimental structure of the same protein · chain A against A, TM-score 0.92

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 P42337
Elsewhere: UniProt P42337 · AlphaFold DB P42337

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