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Crystal structure of trehalose synthase tret mutant E326A from P.HORIKOSHII in complex with udpg
Analyse Crystal structure of trehalose synthase tret mutant E326A from P.HORIKOSHII in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2XA9
- Type
- protein
- Length
- 824 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Trehalose-synthase tret
- UniProt
- O58762
- Ligands
- UPG
- Pockets
- 4 · best druggability 0.73
Structure
x-ray diffraction · 1 distinct chain · 45% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Trehalose-synthase tret | protein | 412 | 45% helix, 14% strand | O58762 |
Ligands and binding sites
- UPG · Uridine-5'-diphosphate-glucose · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1022 | 0.73 | 0.76 | 78 | UPG |
| 2 | 1170 | 0.73 | 0.76 | 80 | empty |
| 3 | 968 | 0.72 | 0.76 | 71 | UPG |
| 4 | 69 | 0.31 | 0.74 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 389 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 covalent (covalent ligand).
Compared structures
- 2XA9 · Crystal structure of trehalose synthase TreT mutant E326A from P. horikoshii in complex… · the same entry in another collection · chain A against A, TM-score 1.00
- O58762 · AlphaFold monomer V2.0 prediction for trehalose synthase (O58762) · a predicted model of the same protein · chain A 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 O58762
- Elsewhere: RCSB PDB 2XA9 · PDBe 2XA9 · UniProt O58762
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