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Leukotriene A4 hydrolase complexed with inhibitor 4-[(2S)-2-{[4-(4- CHLOROPHENOXY)PHENOXY]METHYL}PYRROLIDIN-1-YL]BUTANOATE.

Analyse Leukotriene A4 hydrolase complexed with inhibitor 4-[(2S)-2-{[4-(4… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3FH7
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: 25P, YB, ZN
Pockets: 5 · best druggability 0.85

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Leukotriene a-4 hydrolase (EC 3.3.2.6)	protein	607	43% helix, 23% strand	P09960

Ligands and binding sites

25P · 4-[(2S)-2-{[4-(4-chlorophenoxy)phenoxy]methyl}pyrrolidin-1-yl]butanoate · ligand · chains A
YB · Ytterbium (III) ion · metal · 3 copies · chains A
ZN · Zinc ion · metal · chains A
ACT · Acetate ion · additive · chains A
IMD · Imidazole · additive · chains A
GOL · Glycerol · 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.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1052	0.85	0.86	87	25P
2	106	0.51	0.82	20	empty
3	183	0.48	0.76	26	empty
4	141	0.42	0.75	30	empty
5	78	0.33	0.75	14	empty

Compared structures

3FH7 · Leukotriene A4 Hydrolase complexed with inhibitor… · 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 3FH7 · PDBe 3FH7 · UniProt P09960

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