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INPP5D pandda analysis group deposition -- crystal structure of the phosphatase and C2 domains of SHIP1 in complex with Z2856434856

Analyse INPP5D pandda analysis group deposition -- crystal structure of the phosphatase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5RXW
Type: protein
Length: 460 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 1
EC: 3.1.3.86, 3.1.3.56, 3.1.3.36
UniProt: Q92835
Ligands: T1S
Pockets: 5 · best druggability 0.68

Structure

x-ray diffraction · 1 distinct chain · 17% helix, 37% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 1 (EC 3.1.3.86, 3.1.3.56, 3.1.3.36)	protein	460	17% helix, 37% strand	Q92835

Ligands and binding sites

T1S · 4-[(3-chlorophenyl)methyl]morpholine · ligand · chains A
DMS · Dimethyl sulfoxide · additive · 3 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	398	0.68	0.80	53	DMS
2	93	0.42	0.78	19	DMS
3	92	0.35	0.75	19	empty
4	56	0.32	0.76	18	empty
5	51	0.28	0.75	17	empty

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 Q92835
Elsewhere: RCSB PDB 5RXW · PDBe 5RXW · UniProt Q92835

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