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The crystal structure of the drosophila class III PI3-kinase VPS34

Analyse The crystal structure of the drosophila class III PI3-kinase VPS34 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2X6H
Type: protein
Length: 1,086 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Phosphotidylinositol 3 kinase 59F
EC: 2.7.1.137, 2.7.1.153, 2.7.1.154
UniProt: Q9W1M7
Pockets: 14 · best druggability 0.70

Structure

x-ray diffraction · 2 distinct chains · 58% helix, 8% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Phosphotidylinositol 3 kinase 59F (EC 2.7.1.137, 2.7.1.153, 2.7.1.154)	protein	543	58% helix, 7% strand	Q9W1M7
B	Phosphotidylinositol 3 kinase 59F (EC 2.7.1.137, 2.7.1.153, 2.7.1.154)	protein	543	58% helix, 9% strand	Q9W1M7

Pockets

14 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	754	0.70	0.76	75	empty
2	233	0.69	0.85	28	empty
3	255	0.67	0.83	26	empty
4	211	0.61	0.81	23	empty
5	181	0.53	0.78	26	empty

Interfaces

1 interface between chains.

A–B · 1632 Å² buried · 14 hydrogen bonds · protein-protein

Compared structures

2X6H · The crystal structure of the drosophila class III PI3-kinase VPS34 · 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 Q9W1M7
Elsewhere: RCSB PDB 2X6H · PDBe 2X6H · UniProt Q9W1M7

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