MolNFT v1 · #110638 · protein

Structure of soluble epoxide hydrolase in complex with 1-[3- (TRIFLUOROMETHYL)PYRIDIN-2-YL]PIPERAZINE

4Y2Q · Bifunctional epoxide hydrolase 2: “Structure of soluble epoxide hydrolase in complex with 1-[3- (TRIFLUOROMETHYL)PYRIDIN-2-YL]PIPERAZINE”. X-ray diffraction, 2 ligands (49N, MG), 3 pockets (best druggability 0.84). MolNFT v1 #110638…

PDB: 4Y2Q
Type: protein
Length: 546 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
UniProt: P34913
Ligands: 49N, MG
Pockets: 3 · best druggability 0.84

Structure

x-ray diffraction · 1 distinct chain · 46% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Bifunctional epoxide hydrolase 2 (EC 3.3.2.10)	protein	546	46% helix, 14% strand	P34913

Ligands and binding sites

49N · 1-[3-(trifluoromethyl)pyridin-2-yl]piperazine · ligand · chains A
MG · Magnesium ion · metal · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

3 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	574	0.84	0.89	52	49N
2	471	0.60	0.75	39	empty
3	184	0.57	0.81	27	MG

Compared structures

4Y2Q · Structure of soluble epoxide hydrolase in complex with… · 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 4Y2Q · PDBe 4Y2Q · UniProt P34913

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