Research workbench
[E296Q]LTA4H in complex with arg-ala-arg substrate
Analyse [E296Q]LTA4H in complex with arg-ala-arg substrate in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3B7T
- Type
- protein
- Length
- 613 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Leukotriene a-4 hydrolase; Rar peptide
- EC
- 3.3.2.6, 3.4.11.4
- UniProt
- P09960
- Ligands
- YB, ZN
- Pockets
- 7 · best druggability 0.85
Structure
x-ray diffraction · 2 distinct chains · 43% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Leukotriene a-4 hydrolase (EC 3.3.2.6, 3.4.11.4) | protein | 610 | 43% helix, 23% strand | P09960 |
| B | Rar peptide | protein | 3 | 0% helix, 33% strand | — |
Ligands and binding sites
- YB · Ytterbium (III) ion · metal · 2 copies · chains A
- ZN · Zinc ion · metal · chains A, B
- IMD · Imidazole · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 885 | 0.85 | 0.87 | 76 | IMD |
| 2 | 76 | 0.76 | 0.99 | 19 | empty |
| 3 | 207 | 0.52 | 0.77 | 28 | empty |
| 4 | 93 | 0.51 | 0.83 | 18 | empty |
| 5 | 110 | 0.42 | 0.77 | 22 | empty |
Interfaces
1 interface between chains.
- A–B · 464 Ų buried · 12 hydrogen bonds · protein-protein
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 3B7T · PDBe 3B7T · UniProt P09960
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