Research workbench
Crystal structure of human LTA4H mutant D375N in open conformation (crystal form II)
Analyse Crystal structure of human LTA4H mutant D375N in open conformation (crystal… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5NID
- Type
- protein
- Length
- 609 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
- P09960
- Ligands
- ZN
- Pockets
- 3 · best druggability 0.80
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Leukotriene a-4 hydrolase (EC 3.3.2.6) | protein | 609 | 44% helix, 23% strand | P09960 |
Ligands and binding sites
- ZN · Zinc ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 982 | 0.80 | 0.82 | 84 | empty |
| 2 | 165 | 0.50 | 0.78 | 19 | empty |
| 3 | 69 | 0.31 | 0.74 | 15 | empty |
Compared structures
- 5NID · Crystal structure of human LTA4H mutant D375N in open conformation (crystal form II) · 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 P09960
- Elsewhere: RCSB PDB 5NID · PDBe 5NID · UniProt P09960
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