MolNFT v1 · #19444 · protein
T4 phage B-glucosyltransferase, substrate binding and proposed catalytic mechanism
1QKJ · Beta-glucosyltransferase: “T4 phage B-glucosyltransferase, substrate binding and proposed catalytic mechanism”. X-ray diffraction, 1 ligand (UDP), 3 pockets (best druggability 0.77). MolNFT v1 #19444 on GenesisL1: 3D structure…
- PDB
- 1QKJ
- Type
- protein
- Length
- 351 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 0.77
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Beta-glucosyltransferase (EC 2.4.1.27) | protein | 351 | 39% helix, 18% 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, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 488 | 0.77 | 0.85 | 45 | UDP |
| 2 | 135 | 0.54 | 0.82 | 21 | empty |
| 3 | 128 | 0.42 | 0.75 | 24 | empty |
Compared structures
- 1QKJ · T4 Phage B-Glucosyltransferase, Substrate Binding and Proposed Catalytic Mechanism · 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 1QKJ · PDBe 1QKJ · UniProt P04547
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