Research workbench
Structure of human leukotriene A4 hydrolase in complex with inhibitor captopril
Analyse Structure of human leukotriene A4 hydrolase in complex with inhibitor captopril in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4DPR
- Type
- protein
- Length
- 607 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
- X8Z, YB, ZN
- Pockets
- 5 · best druggability 0.86
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Leukotriene a-4 hydrolase (EC 3.3.2.6) | protein | 607 | 44% helix, 24% strand | P09960 |
Ligands and binding sites
- X8Z · L-captopril · ligand · chains A
- YB · Ytterbium (III) ion · metal · 5 copies · chains A
- ZN · Zinc ion · metal · chains A
- GOL · Glycerol · additive · 2 copies · chains A
- ACY · Acetic acid · 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 | 1008 | 0.86 | 0.87 | 90 | X8Z |
| 2 | 106 | 0.50 | 0.81 | 18 | empty |
| 3 | 198 | 0.49 | 0.76 | 27 | empty |
| 4 | 173 | 0.48 | 0.77 | 27 | empty |
| 5 | 50 | 0.26 | 0.74 | 15 | empty |
Compared structures
- 4DPR · Structure of human Leukotriene A4 hydrolase in complex with inhibitor captopril · the same entry in another collection · chain A against A, TM-score 1.00
- P09960 · AlphaFold monomer V2.0 prediction for leukotriene a-4 hydrolase (P09960) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 4DPR · PDBe 4DPR · UniProt P09960
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