MolNFT v1 · #113650 · protein

Ligand complex structure of soluble epoxide hydrolase

5ALS · Bifunctional epoxide hydrolase 2: “Ligand complex structure of soluble epoxide hydrolase”. X-ray diffraction, 2 ligands (5DQ, SO4), 5 pockets (best druggability 0.79). MolNFT v1 #113650 on GenesisL1: 3D structure, binding sites and…

PDB: 5ALS
Type: protein
Length: 541 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Bifunctional epoxide hydrolase 2
EC: 3.3.2.10, 3.1.3.76
UniProt: P34913
Ligands: 5DQ, SO4
Pockets: 5 · best druggability 0.79

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Bifunctional epoxide hydrolase 2 (EC 3.3.2.10, 3.1.3.76)	protein	541	45% helix, 14% strand	P34913

Ligands and binding sites

5DQ · N-cyclopentyl-2-[4-(trifluoromethyl)phenyl]-3H-imidazo[4,5-b]pyridine-7-sulfonamide · ligand · chains A
SO4 · Sulfate ion · ion · 3 copies · 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	632	0.79	0.84	58	SO4, 5DQ
2	186	0.60	0.82	32	empty
3	458	0.58	0.74	37	empty
4	51	0.34	0.78	14	empty
5	53	0.27	0.74	12	empty

Compared structures

5ALS · ligand complex structure of soluble epoxide hydrolase · 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 P34913
Elsewhere: RCSB PDB 5ALS · PDBe 5ALS · UniProt P34913

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.