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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
- 5ONN
- Type
- protein
- Length
- 138 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- L-ectoine synthase
- EC
- 4.2.1.108
- UniProt
- A0A1R1AV52
- Ligands
- 9YT, FE
- Pockets
- 1 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 9% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | L-ectoine synthase (EC 4.2.1.108) | protein | 138 | 9% helix, 41% strand | A0A1R1AV52 |
Ligands and binding sites
- 9YT · (2~{S})-4-acetamido-2-azanyl-butanoic acid · ligand · chains A
- FE · Fe (III) ion · metal · chains A
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 | 95 | 0.79 | 0.99 | 24 | FE, 9YT |
Compared structures
- 5ONN · 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 5ONN · PDBe 5ONN · UniProt A0A1R1AV52
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