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Crystal structure of the DNA modifying enzyme beta-glucosyltransferase in the presence and absence of the substrate uridine diphosphoglucose

Analyse Crystal structure of the DNA modifying enzyme beta-glucosyltransferase in the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2BGU
Type: protein
Length: 328 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Beta-glucosyltransferase
EC: 2.4.1.27
UniProt: P04547
Ligands: UDP
Pockets: 3 · best druggability 0.79

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Beta-glucosyltransferase (EC 2.4.1.27)	protein	328	39% helix, 19% strand	P04547

Ligands and binding sites

UDP · Uridine-5'-diphosphate · ligand · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	512	0.79	0.86	48	UDP
2	122	0.49	0.79	21	empty
3	155	0.46	0.76	26	empty

Compared structures

2BGU · Crystal structure of the DNA modifying enzyme beta-glucosyltransferase in the presence… · 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 P04547
Elsewhere: RCSB PDB 2BGU · PDBe 2BGU · UniProt P04547

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