Research workbench
Crystal structure of the mutb E254Q mutant in complex with the substrate sucrose
Analyse Crystal structure of the mutb E254Q mutant in complex with the substrate sucrose in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2PWE
- Type
- protein
- Length
- 1,112 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Sucrose isomerase
- EC
- 5.4.99.11
- UniProt
- Q2PS28
- Ligands
- GLC, FRU, CA
- Pockets
- 10 · best druggability 0.77
Structure
x-ray diffraction · 1 distinct chain · 33% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Sucrose isomerase (EC 5.4.99.11) | protein | 556 | 33% helix, 19% strand | Q2PS28 |
Ligands and binding sites
- GLC · alpha-D-glucopyranose · sugar · 2 copies · chains A, B
- FRU · beta-D-fructofuranose · sugar · 2 copies · chains A, B
- CA · Calcium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 96 | 0.77 | 0.98 | 21 | GLC, FRU |
| 2 | 103 | 0.77 | 0.97 | 22 | GLC, FRU |
| 3 | 249 | 0.58 | 0.79 | 24 | empty |
| 4 | 207 | 0.55 | 0.78 | 27 | empty |
| 5 | 171 | 0.46 | 0.75 | 24 | empty |
Interfaces
1 interface between chains.
- A–B · 226 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 2PWE · Crystal structure of the MutB E254Q mutant in complex with the substrate sucrose · 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 Q2PS28
- Elsewhere: RCSB PDB 2PWE · PDBe 2PWE · UniProt Q2PS28
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