Research workbench
Structure of native leukotriene A4 hydrolase from saccharomyces cerevisiae
Analyse Structure of native leukotriene A4 hydrolase from saccharomyces cerevisiae in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2XPY
- Type
- protein
- Length
- 628 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Leukotriene a-4 hydrolase
- EC
- 3.3.2.6
- UniProt
- Q10740
- Ligands
- GSH, ZN
- Pockets
- 4 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Leukotriene a-4 hydrolase (EC 3.3.2.6) | protein | 628 | 43% helix, 19% strand | Q10740 |
Ligands and binding sites
- GSH · Glutathione · ligand · chains A
- ZN · Zinc ion · metal · chains A
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1049 | 0.75 | 0.78 | 89 | empty |
| 2 | 205 | 0.50 | 0.76 | 30 | empty |
| 3 | 99 | 0.40 | 0.76 | 15 | empty |
| 4 | 51 | 0.32 | 0.77 | 19 | empty |
Modifications
Observed in the structure: 1 covalent (covalent ligand).
Compared structures
- 2XPY · Structure of Native Leukotriene A4 Hydrolase from Saccharomyces cerevisiae · the same entry in another collection · chain A against A, TM-score 1.00
- Q10740 · AlphaFold monomer V2.0 prediction for leucine aminopeptidase 2 (Q10740) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 Q10740
- Elsewhere: RCSB PDB 2XPY · PDBe 2XPY · UniProt Q10740
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