Research workbench
Crystal Structure of Ectoine Synthase from P. lautus
Analyse Crystal Structure of Ectoine Synthase from P. lautus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5ONM
- Type
- protein
- Length
- 138 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.52
- Source
- Paenibacillus lautus
- Molecule
- L-ectoine synthase
- EC
- 4.2.1.108
- UniProt
- A0A1R1AV52
- Ligands
- FE, SO4
- Pockets
- 1 · best druggability 0.74
Structure
x-ray diffraction · resolution 1.52 · 1 distinct chain · 9% helix, 43% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | L-ectoine synthase (EC 4.2.1.108) | protein | 138 | 9% helix, 43% strand | A0A1R1AV52 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 104 | 0.74 | 0.95 | 29 | empty |
Compared structures
- 5ONM · Crystal structure of ectoine synthase from P. lautus · 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 A0A1R1AV52
- Elsewhere: RCSB PDB 5ONM · PDBe 5ONM · UniProt A0A1R1AV52
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