MolNFT v1 · #25243 · protein

Crystal structure of alpha-glucosidase (TM0752) from thermotoga maritima at 2.50 a resolution

1VJT: “Crystal structure of alpha-glucosidase (TM0752) from thermotoga maritima at 2.50 a resolution”. X-ray diffraction, 1 ligand (NAD), 1 pocket (best druggability 0.78). MolNFT v1 #25243 on GenesisL1: 3D structure, binding sites and…

PDB: 1VJT
Type: protein
Length: 471 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Alpha-glucosidase
EC: 3.2.1.139
UniProt: Q9WZL1
Ligands: NAD
Pockets: 1 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 47% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Alpha-glucosidase (EC 3.2.1.139)	protein	471	47% helix, 15% strand	Q9WZL1

Ligands and binding sites

NAD · Nicotinamide-adenine-dinucleotide · 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	993	0.78	0.80	76	NAD

Modifications

Observed in the structure: 15 modified (engineered).

Compared structures

1VJT · Crystal structure of Alpha-glucosidase (TM0752) from Thermotoga maritima at 2.50 A… · the same entry in another collection · 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 Q9WZL1
Elsewhere: RCSB PDB 1VJT · PDBe 1VJT · UniProt Q9WZL1

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