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Structure of human leukotriene A4 hydrolase in complex with inhibitor 4AZ

Analyse Structure of human leukotriene A4 hydrolase in complex with inhibitor 4AZ in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5BPP
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: A4Z, YB, ZN
Pockets: 4 · best druggability 0.86

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	607	44% helix, 23% strand	P09960

Ligands and binding sites

A4Z · 2-(4-butoxyphenyl)-N-hydroxyacetamide · ligand · chains A
YB · Ytterbium (III) ion · metal · 3 copies · chains A
ZN · Zinc ion · metal · chains A
ACT · Acetate ion · additive

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.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	988	0.86	0.87	81	A4Z
2	105	0.54	0.84	21	empty
3	190	0.52	0.77	27	empty
4	126	0.42	0.76	28	empty

Compared structures

5BPP · Structure of human Leukotriene A4 hydrolase in complex with inhibitor 4AZ · 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 5BPP · PDBe 5BPP · UniProt P09960

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