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AlphaFold monomer V2.0 prediction for phosphatidylinositide phosphatase SAC2 (Q9Y2H2)

Analyse AlphaFold monomer V2.0 prediction for phosphatidylinositide phosphatase SAC2… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession: Q9Y2H2
Type: protein
Length: 1,132 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0x6DAA77C4263E74E745cA9c4D8E291e57e8991Cf5
Molecule: Phosphatidylinositide phosphatase SAC2
UniProt: Q9Y2H2
Pockets: 13 · best druggability 0.77

Structure

1 distinct chain · 28% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Phosphatidylinositide phosphatase SAC2	protein	1132	28% helix, 17% strand	Q9Y2H2

Pockets

13 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	87	0.77	0.99	23	empty
2	347	0.69	0.82	39	empty
3	617	0.67	0.76	58	empty
4	403	0.59	0.75	38	empty
5	179	0.58	0.81	18	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

4XUU · The hSac2 domain from human phosphoinositide phosphatase Sac2 · an experimental structure of the same protein · chain A against B, TM-score 0.15
4XUU · The HSAC2 domain from human phosphoinositide phosphatase SAC2 · an experimental structure of the same protein · chain A against A, TM-score 0.15

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 Q9Y2H2
Elsewhere: UniProt Q9Y2H2 · AlphaFold DB Q9Y2H2

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