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Crystal structure of T4 phage bgt in complex with its udp-glucose substrate

Analyse Crystal structure of T4 phage bgt in complex with its udp-glucose substrate in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1J39
Type
protein
Length
344 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
DNA beta-glucosyltransferase
EC
2.4.1.27
UniProt
P04547
Ligands
UPG
Pockets
3 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 17% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ADNA beta-glucosyltransferase (EC 2.4.1.27)protein34438% helix, 17% strandP04547

Ligands and binding sites

  • UPG · Uridine-5'-diphosphate-glucose · ligand · chains A
  • GOL · Glycerol · additive · 3 copies · 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, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14910.760.8447UPG
21360.520.8020empty
31720.480.7630empty

Compared structures

  • 1J39 · Crystal Structure of T4 phage BGT in complex with its UDP-glucose substrate · the same entry in another collection · chain A against A, TM-score 1.00

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