Research workbench
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
- 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.
| Volume (ų) | 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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