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The complex structure of beta-1,2-glucosyltransferase from ignavibacterium album with phenyl alpha-D-glucoside
Analyse The complex structure of beta-1,2-glucosyltransferase from ignavibacterium… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7VL3
- Type
- protein
- Length
- 1,411 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Beta-1,2-glucosyltransferase
- UniProt
- I0AIT9
- Ligands
- 7OL, CA
- Pockets
- 17 · best druggability 0.82
Structure
x-ray diffraction · 2 distinct chains · 36% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Beta-1,2-glucosyltransferase | protein | 707 | 36% helix, 24% strand | I0AIT9 |
| B | Beta-1,2-glucosyltransferase | protein | 704 | 36% helix, 24% strand | I0AIT9 |
Ligands and binding sites
- 7OL · (2R,3S,4S,5R,6R)-2-(hydroxymethyl)-6-phenoxy-oxane-3,4, 5-triol · ligand · 2 copies · chains A, B
- CA · Calcium ion · metal · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
17 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1045 | 0.82 | 0.83 | 118 | 7OL |
| 2 | 310 | 0.74 | 0.86 | 49 | 7OL |
| 3 | 367 | 0.66 | 0.80 | 55 | empty |
| 4 | 339 | 0.66 | 0.81 | 55 | empty |
| 5 | 296 | 0.56 | 0.76 | 44 | empty |
Interfaces
1 interface between chains.
- A–B · 1834 Ų buried · 23 hydrogen bonds · protein-protein
Compared structures
- 7VL3 · The complex structure of beta-1,2-glucosyltransferase from Ignavibacterium album with… · 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 I0AIT9
- Elsewhere: RCSB PDB 7VL3 · PDBe 7VL3 · UniProt I0AIT9
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