MolNFT v1 · #174646 · protein

Glycosidase F290Y at PH8.0

7C24 · Isomaltose glucohydrolase: “Glycosidase F290Y at PH8.0”. X-ray diffraction, 1 ligand (NH4), 1 pocket (best druggability 0.63). MolNFT v1 #174646 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 7C24
Type: protein
Length: 372 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Isomaltose glucohydrolase
EC: 3.2.1.205
UniProt: D2PPM8
Ligands: NH4
Pockets: 1 · best druggability 0.63

Structure

x-ray diffraction · 1 distinct chain · 56% helix, 5% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Isomaltose glucohydrolase (EC 3.2.1.205)	protein	372	56% helix, 5% strand	D2PPM8

Ligands and binding sites

NH4 · Ammonium ion · ion · chains A
GOL · Glycerol · additive · 5 copies · 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	175	0.63	0.83	24	GOL

Modifications

Observed in the structure: 1 modified (oxidation).

Compared structures

7C24 · Glycosidase F290Y at pH8.0 · the same entry in another collection · chain A against A, TM-score 1.00
D2PPM8 · AlphaFold monomer V2.0 prediction for isomaltose glucohydrolase (D2PPM8) · a predicted model of the same protein · 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 D2PPM8
Elsewhere: RCSB PDB 7C24 · PDBe 7C24 · UniProt D2PPM8

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