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Structure of human SHP2 in complex with compound 16

Analyse Structure of human SHP2 in complex with compound 16 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7R75
Type: protein
Length: 494 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Tyrosine-protein phosphatase non-receptor type 11
EC: 3.1.3.48
UniProt: Q06124
Ligands: 33I
Pockets: 4 · best druggability 0.61

Structure

x-ray diffraction · 1 distinct chain · 30% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Tyrosine-protein phosphatase non-receptor type 11 (EC 3.1.3.48)	protein	494	30% helix, 25% strand	Q06124

Ligands and binding sites

33I · 6-(4-amino-4-methylpiperidin-1-yl)-3-(3-chlorophenyl)-1,5-dihydro-4H-pyrazolo[3,4-d]pyrimidin-4-one · ligand · chains A

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

Pockets

4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	313	0.61	0.79	32	33I
2	195	0.54	0.79	38	empty
3	148	0.51	0.79	20	empty
4	64	0.28	0.73	13	empty

Compared structures

7R75 · Structure of human SHP2 in complex with compound 16 · 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 Q06124
Elsewhere: RCSB PDB 7R75 · PDBe 7R75 · UniProt Q06124

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