Research workbench
Crystal structure of the enol-lactonase from burkholderia xenovorans LB400
Analyse Crystal structure of the enol-lactonase from burkholderia xenovorans LB400 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2XUA
- Type
- protein
- Length
- 521 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 3-oxoadipate enol-lactonase
- EC
- 3.1.1.24
- UniProt
- Q13KT2
- Ligands
- SHF
- Pockets
- 7 · best druggability 0.75
Structure
x-ray diffraction · 2 distinct chains · 50% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 3-oxoadipate enol-lactonase (EC 3.1.1.24) | protein | 260 | 50% helix, 17% strand | Q13KT2 |
| H | 3-oxoadipate enol-lactonase (EC 3.1.1.24) | protein | 261 | 49% helix, 18% strand | Q13KT2 |
Ligands and binding sites
- SHF · Laevulinic acid · ligand · chains H
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 | 92 | 0.75 | 0.97 | 21 | empty |
| 2 | 63 | 0.65 | 0.93 | 19 | SHF |
| 3 | 64 | 0.60 | 0.90 | 17 | empty |
| 4 | 172 | 0.46 | 0.75 | 33 | empty |
| 5 | 104 | 0.43 | 0.78 | 21 | empty |
Interfaces
1 interface between chains.
- A–H · 1061 Ų buried · 18 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 13 modified (engineered).
Compared structures
- 2XUA · Crystal structure of the enol-lactonase from Burkholderia xenovorans LB400 · 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 Q13KT2
- Elsewhere: RCSB PDB 2XUA · PDBe 2XUA · UniProt Q13KT2
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