Research workbench
Structure of yeast LTA4 hydrolase in complex with bestatin
Analyse Structure of yeast LTA4 hydrolase in complex with bestatin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2XQ0
- Type
- protein
- Length
- 625 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
- BES, ZN, CL
- Pockets
- 8 · best druggability 0.80
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 | 625 | 43% helix, 19% strand | Q10740 |
Ligands and binding sites
- BES · 2-(3-amino-2-hydroxy-4-phenyl-butyrylamino)-4-methyl-pentanoic acid · ligand · chains A
- ZN · Zinc ion · metal · chains A
- CL · Chloride ion · ion · 4 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1122 | 0.80 | 0.81 | 72 | BES |
| 2 | 132 | 0.43 | 0.76 | 20 | empty |
| 3 | 117 | 0.42 | 0.76 | 26 | empty |
| 4 | 68 | 0.42 | 0.80 | 14 | empty |
| 5 | 129 | 0.41 | 0.75 | 20 | 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 Q10740
- Elsewhere: RCSB PDB 2XQ0 · PDBe 2XQ0 · UniProt Q10740
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