Research workbench
Leukotriene A4 Hydrolase complexed with inhibitor N-[3-(4-benzylphenoxy)propyl]-N-methyl-beta-alanine.
Analyse Leukotriene A4 Hydrolase complexed with inhibitor… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3FHE
- Type
- protein
- Length
- 607 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.16
- Source
- Homo sapiens
- Molecule
- Leukotriene A-4 hydrolase
- EC
- 3.3.2.6
- UniProt
- P09960
- Ligands
- 28P, YB, ZN
- Pockets
- 5 · best druggability 0.86
Structure
x-ray diffraction · resolution 2.16 · 1 distinct chain · 43% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Leukotriene A-4 hydrolase (EC 3.3.2.6) | protein | 607 | 43% helix, 23% strand | P09960 |
Ligands and binding sites
- 28P · N-[3-(4-benzylphenoxy)propyl]-N-methyl-beta-alanine · ligand · chains A
- YB · Ytterbium (III) ion · metal · 3 copies · chains A
- ZN · Zinc ion · metal · chains A
- ACT · Acetate ion · additive · chains A
- IMD · Imidazole · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 997 | 0.86 | 0.86 | 89 | 28P |
| 2 | 101 | 0.50 | 0.82 | 20 | empty |
| 3 | 178 | 0.48 | 0.76 | 26 | empty |
| 4 | 140 | 0.40 | 0.74 | 27 | empty |
| 5 | 57 | 0.31 | 0.76 | 13 | empty |
Compared structures
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 P09960
- Elsewhere: RCSB PDB 3FHE · PDBe 3FHE · UniProt P09960
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