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Crystal structure of human SHIP2

Analyse Crystal structure of human SHIP2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3NR8
Type: protein
Length: 592 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase 2
EC: 3.1.3.1
UniProt: O15357
Ligands: CL
Pockets: 7 · best druggability 0.51

Structure

x-ray diffraction · 2 distinct chains · 21% helix, 33% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B	Phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase 2 (EC 3.1.3.1)	protein	299	20% helix, 33% strand	O15357
A	Phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase 2 (EC 3.1.3.1)	protein	293	22% helix, 33% strand	O15357

Ligands and binding sites

CL · Chloride ion · ion · chains B

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

Pockets

7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	83	0.51	0.83	17	empty
2	62	0.51	0.85	17	empty
3	227	0.49	0.75	21	empty
4	202	0.47	0.75	21	empty
5	113	0.36	0.74	24	CL

Interfaces

1 interface between chains.

B–A · 548 Å² buried · 6 hydrogen bonds · protein-protein

Compared structures

3NR8 · Crystal structure of human SHIP2 · the same entry in another collection · chain B against B, TM-score 1.00
O15357 · AlphaFold monomer V2.0 prediction for phosphatidylinositol 3,4,5-trisphosphate… · 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 O15357
Elsewhere: RCSB PDB 3NR8 · PDBe 3NR8 · UniProt O15357

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