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Catalytic domain of human SHP2

Analyse Catalytic domain of human SHP2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3ZM3
Type
protein
Length
267 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
Pockets
3 · best druggability 0.37

Structure

x-ray diffraction · 1 distinct chain · 33% helix, 21% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ATyrosine-protein phosphatase non-receptor type 11 (EC 3.1.3.48)protein26733% helix, 21% strandQ06124

Pockets

3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1540.370.8017empty
2950.360.7522empty
3900.350.7520empty

Compared structures

  • 3ZM3 · Catalytic domain of human SHP2 · the same entry in another collection · chain A against A, TM-score 1.00

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