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LTA4 hydrolase in complex with COMPOUND11

Analyse LTA4 hydrolase in complex with COMPOUND11 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6ENC
Type: protein
Length: 608 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: BGW, YB, ZN
Pockets: 5 · best druggability 0.86

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Leukotriene a-4 hydrolase (EC 3.3.2.6)	protein	608	43% helix, 24% strand	P09960

Ligands and binding sites

BGW · 1-[[4-(1,3-benzothiazol-2-yloxy) phenyl]methyl]piperidine-4-carboxylic acid · ligand · chains A
YB · Ytterbium (III) ion · metal · 2 copies · chains A
ZN · Zinc ion · metal · chains A
IMD · Imidazole · additive · 2 copies · chains A
ACT · Acetate ion · 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, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1040	0.86	0.86	89	ZN, IMD, BGW
2	199	0.51	0.77	30	empty
3	91	0.50	0.83	21	empty
4	133	0.42	0.76	27	empty
5	93	0.37	0.75	22	empty

Compared structures

6ENC · LTA4 hydrolase in complex with Compound11 · 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 6ENC · PDBe 6ENC · UniProt P09960

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