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The complex structure of beta-1,2-glucosyltransferase from Ignavibacterium album with methyl 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
- 7VL1
- Type
- protein
- Length
- 1,408 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.6
- Source
- Ignavibacterium album (strain DSM 19864 / JCM 16511 / NBRC 101810 / Mat9-16)
- Molecule
- beta-1,2-glucosyltransferase
- UniProt
- I0AIT9
- Ligands
- GYP, CA
- Pockets
- 17 · best druggability 0.82
Structure
x-ray diffraction · resolution 1.6 · 2 distinct chains · 36% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | beta-1,2-glucosyltransferase | protein | 706 | 35% helix, 25% strand | I0AIT9 |
| B | beta-1,2-glucosyltransferase | protein | 702 | 36% helix, 24% strand | I0AIT9 |
Ligands and binding sites
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 | 1092 | 0.82 | 0.83 | 119 | GYP |
| 2 | 324 | 0.73 | 0.85 | 48 | empty |
| 3 | 357 | 0.66 | 0.80 | 55 | empty |
| 4 | 378 | 0.66 | 0.80 | 57 | empty |
| 5 | 299 | 0.56 | 0.76 | 42 | empty |
Interfaces
1 interface between chains.
- A–B · 1909 Ų buried · 24 hydrogen bonds · protein-protein
Compared structures
- 7VL1 · 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 7VL1 · PDBe 7VL1 · UniProt I0AIT9
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