MolNFT v1 · #30996 · protein

Crystal structure of mouse GM2- activator protein

2AGC · Ganglioside GM2 activator: “Crystal structure of mouse GM2- activator protein”. X-ray diffraction, 2 ligands (DAO, MYR), 1 pocket (best druggability 0.81). MolNFT v1 #30996 on GenesisL1: 3D structure, binding sites and pockets in…

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).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ganglioside GM2 activator	protein	162	9% helix, 48% strand	Q60648

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.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1154	0.81	0.81	71	MYR, 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

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 Q60648
Elsewhere: RCSB PDB 2AGC · PDBe 2AGC · UniProt Q60648

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