Research workbench
Trehalose-6-phosphate from E. COLI bound with udp-glucose.
Analyse Trehalose-6-phosphate from E. COLI bound with udp-glucose. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1UQU
- Type
- protein
- Length
- 901 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha, alpha-trehalose-phosphate synthase
- EC
- 2.4.1.15
- UniProt
- P31677
- Ligands
- UPG
- Pockets
- 8 · best druggability 0.77
Structure
x-ray diffraction · 2 distinct chains · 47% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alpha, alpha-trehalose-phosphate synthase (EC 2.4.1.15) | protein | 452 | 48% helix, 20% strand | P31677 |
| B | Alpha, alpha-trehalose-phosphate synthase (EC 2.4.1.15) | protein | 449 | 46% helix, 18% strand | P31677 |
Ligands and binding sites
- UPG · Uridine-5'-diphosphate-glucose · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 814 | 0.77 | 0.80 | 48 | UPG |
| 2 | 87 | 0.73 | 0.95 | 16 | empty |
| 3 | 789 | 0.72 | 0.78 | 48 | empty |
| 4 | 184 | 0.65 | 0.85 | 32 | empty |
| 5 | 387 | 0.64 | 0.78 | 44 | empty |
Interfaces
1 interface between chains.
- A–B · 1068 Ų buried · 16 hydrogen bonds · protein-protein
Compared structures
- 1UQU · Trehalose-6-phosphate from E. coli bound with UDP-glucose. · the same entry in another collection · chain A against A, TM-score 1.00
- P31677 · AlphaFold monomer V2.0 prediction for trehalose-6-phosphate synthase (P31677) · a predicted model of the same protein · chain B against A, TM-score 0.99
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 P31677
- Elsewhere: RCSB PDB 1UQU · PDBe 1UQU · UniProt P31677
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