Research workbench
Crystal structure of levansucrase from gluconacetobacter diazotrophicus
Analyse Crystal structure of levansucrase from gluconacetobacter diazotrophicus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1W18
- Type
- protein
- Length
- 985 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Levansucrase
- EC
- 2.4.1.10
- UniProt
- Q43998
- Ligands
- SO4
- Pockets
- 7 · best druggability 0.68
Structure
x-ray diffraction · 2 distinct chains · 10% helix, 40% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Levansucrase (EC 2.4.1.10) | protein | 492 | 10% helix, 40% strand | Q43998 |
| B | Levansucrase (EC 2.4.1.10) | protein | 493 | 9% helix, 40% strand | Q43998 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 499 | 0.68 | 0.79 | 51 | empty |
| 2 | 520 | 0.67 | 0.78 | 48 | empty |
| 3 | 287 | 0.58 | 0.78 | 31 | empty |
| 4 | 62 | 0.45 | 0.83 | 19 | empty |
| 5 | 61 | 0.41 | 0.81 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 267 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
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 Q43998
- Elsewhere: RCSB PDB 1W18 · PDBe 1W18 · UniProt Q43998
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