MolNFT v1 · #32120 · protein

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

2BGT: “Crystal structure of the DNA modifying enzyme beta-glucosyltransferase in the presence and absence of the…”. X-ray diffraction, 3 pockets (best druggability 0.77). MolNFT v1 #32120 on GenesisL1: 3D structure, binding sites and…

PDB: 2BGT
Type: protein
Length: 329 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
Pockets: 3 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Beta-glucosyltransferase (EC 2.4.1.27)	protein	329	36% helix, 18% strand	P04547

Pockets

3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	544	0.77	0.84	43	empty
2	171	0.54	0.79	20	empty
3	99	0.36	0.74	16	empty

Compared structures

2BGT · 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 2BGT · PDBe 2BGT · UniProt P04547

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