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Crystal structure analysis of the human leukotriene A4 hydrolase

Analyse Crystal structure analysis of the human leukotriene A4 hydrolase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4RVB
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
YB, ZN
Pockets
4 · best druggability 0.86

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 24% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ALeukotriene a-4 hydrolase (EC 3.3.2.6)protein60744% helix, 24% strandP09960

Ligands and binding sites

  • YB · Ytterbium (III) ion · metal · chains A
  • ZN · Zinc ion · metal · chains A
  • IMD · Imidazole · additive · 3 copies · chains A
  • ACT · Acetate ion · additive · 2 copies · chains A
  • GOL · Glycerol · additive · 2 copies · chains A
  • ACY · Acetic acid · additive · 2 copies · 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, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110010.860.8692ACT, IMD, ACY
22110.520.7727empty
3930.510.8318empty
41200.390.7526empty

Compared structures

  • 4RVB · Crystal Structure Analysis of the Human Leukotriene A4 Hydrolase · the same entry in another collection · chain A against A, TM-score 1.00

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