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The crystal structure of erwinia tasmaniensis levansucrase in complex with (S)-1,2,4-butanentriol
Analyse The crystal structure of erwinia tasmaniensis levansucrase in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7OSO
- Type
- protein
- Length
- 412 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Levansucrase (beta-D-fructofuranosyl transferase)
- EC
- 2.4.1.10
- UniProt
- B2VCC3
- Ligands
- 0V1, ZN
- Pockets
- 2 · best druggability 0.54
Structure
x-ray diffraction · 1 distinct chain · 7% helix, 47% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Levansucrase (beta-D-fructofuranosyl transferase) (EC 2.4.1.10) | protein | 412 | 7% helix, 47% strand | B2VCC3 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 226 | 0.54 | 0.77 | 37 | ZN, 0V1 |
| 2 | 62 | 0.28 | 0.73 | 15 | empty |
Compared structures
- 7OSO · The crystal structure of Erwinia tasmaniensis levansucrase in complex 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 B2VCC3
- Elsewhere: RCSB PDB 7OSO · PDBe 7OSO · UniProt B2VCC3
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