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Crystal structure of mouse GM2- activator protein

Analyse Crystal structure of mouse GM2- activator protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2AGC
Type
protein
Length
162 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Ganglioside GM2 activator
UniProt
Q60648
Ligands
DAO, MYR
Pockets
1 · best druggability 0.81

Structure

x-ray diffraction · 1 distinct chain · 9% helix, 48% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AGanglioside GM2 activatorprotein1629% helix, 48% strandQ60648

Ligands and binding sites

  • DAO · Lauric acid · ligand · 2 copies · chains A
  • MYR · Myristic acid · ligand · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111540.810.8171MYR, DAO

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

  • 2AGC · Crystal Structure of mouse GM2- activator Protein · the same entry in another collection · chain A against A, TM-score 1.00
  • Q60648 · AlphaFold monomer V2.0 prediction for ganglioside GM2 activator (Q60648) · a predicted model of the same protein · chain A against A, TM-score 0.95

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