Research workbench
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).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA beta-glucosyltransferase (EC 2.4.1.27) | protein | 344 | 38% helix, 17% strand | P04547 |
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.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 491 | 0.76 | 0.84 | 47 | UPG |
| 2 | 136 | 0.52 | 0.80 | 20 | empty |
| 3 | 172 | 0.48 | 0.76 | 30 | empty |
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
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 1J39 · PDBe 1J39 · UniProt P04547
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