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Structure of native yeast LTA4 hydrolase
Analyse Structure of native yeast LTA4 hydrolase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2XPZ
- Type
- protein
- Length
- 627 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
- ZN
- Pockets
- 4 · best druggability 0.74
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Leukotriene a-4 hydrolase (EC 3.3.2.6) | protein | 627 | 40% helix, 19% strand | Q10740 |
Ligands and binding sites
- ZN · Zinc ion · metal · chains A
- BU3 · (R,R)-2,3-butanediol · additive · chains A
- 15P · Polyethylene glycol (N=34) · 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 | 1004 | 0.74 | 0.77 | 70 | empty |
| 2 | 138 | 0.48 | 0.78 | 22 | empty |
| 3 | 133 | 0.40 | 0.74 | 16 | empty |
| 4 | 61 | 0.35 | 0.78 | 15 | BU3 |
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 2XPZ · PDBe 2XPZ · UniProt Q10740
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