MolNFT v1 · #18603 · protein

GM2-activator protein crystal structure

1PUB: “GM2-activator protein crystal structure”. X-ray diffraction, 1 ligand (3PH), 1 pocket (best druggability 0.75). MolNFT v1 #18603 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1PUB
Type: protein
Length: 162 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: GM2-activator protein
UniProt: P17900
Ligands: 3PH
Pockets: 1 · best druggability 0.75

Structure

x-ray diffraction · 1 distinct chain · 9% helix, 52% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	GM2-activator protein	protein	162	9% helix, 52% strand	P17900

Ligands and binding sites

3PH · 1,2-diacyl-glycerol-3-sn-phosphate · 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	992	0.75	0.77	70	3PH

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

1PUB · GM2-activator Protein crystal structure · the same entry in another collection · chain A against A, TM-score 1.00
P17900 · AlphaFold monomer V2.0 prediction for ganglioside GM2 activator (P17900) · 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 P17900
Elsewhere: RCSB PDB 1PUB · PDBe 1PUB · UniProt P17900

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