Research workbench
A new target for shigellosis: rational design and crystallographic studies of inhibitors of tRNA-guanine transglycosylase
Analyse A new target for shigellosis: rational design and crystallographic studies of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1ENU
- Type
- protein
- Length
- 372 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- TRNA-guanine transglycosylase
- EC
- 2.4.2.29
- UniProt
- P28720
- Ligands
- APZ, ZN
- Pockets
- 2 · best druggability 0.68
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | TRNA-guanine transglycosylase (EC 2.4.2.29) | protein | 372 | 44% helix, 19% strand | P28720 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 294 | 0.68 | 0.83 | 51 | APZ |
| 2 | 76 | 0.37 | 0.77 | 18 | empty |
Compared structures
- 1ENU · A new target for shigellosis: Rational design and crystallographic studies of inhibitors… · 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 P28720
- Elsewhere: RCSB PDB 1ENU · PDBe 1ENU · UniProt P28720
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