Research workbench
Crystal structure of the trehalulose synthase mutant, mutb D415N, in complex with tris
Analyse Crystal structure of the trehalulose synthase mutant, mutb D415N, in complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4GO9
- Type
- protein
- Length
- 1,109 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Sucrose isomerase
- EC
- 5.4.11.99
- UniProt
- Q2PS28
- Ligands
- CA
- Pockets
- 8 · best druggability 0.76
Structure
x-ray diffraction · 2 distinct chains · 33% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Sucrose isomerase (EC 5.4.11.99) | protein | 555 | 34% helix, 19% strand | Q2PS28 |
| B | Sucrose isomerase (EC 5.4.11.99) | protein | 554 | 33% helix, 19% strand | Q2PS28 |
Ligands and binding sites
- CA · Calcium ion · metal · 2 copies · chains A, B
- TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 86 | 0.76 | 0.98 | 21 | TRS |
| 2 | 84 | 0.73 | 0.96 | 21 | TRS |
| 3 | 337 | 0.61 | 0.78 | 37 | empty |
| 4 | 271 | 0.58 | 0.78 | 36 | empty |
| 5 | 152 | 0.45 | 0.76 | 24 | empty |
Interfaces
1 interface between chains.
- A–B · 228 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 4GO9 · CRYSTAL STRUCTURE of the TREHALULOSE SYNTHASE MUTANT, MUTB D415N, in COMPLEX with TRIS · 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 4GO9 · PDBe 4GO9 · UniProt Q2PS28
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