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Crystal structure of soluble epoxide hydrolase

Analyse Crystal structure of soluble epoxide hydrolase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3I1Y
Type: protein
Length: 545 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Epoxide hydrolase 2
EC: 3.3.2.10
UniProt: P34913
Ligands: 33N
Pockets: 5 · best druggability 0.83

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Epoxide hydrolase 2 (EC 3.3.2.10)	protein	545	45% helix, 15% strand	P34913

Ligands and binding sites

33N · N-(3,3-diphenylpropyl)pyridine-3-carboxamide · ligand · 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	625	0.83	0.87	59	33N
2	194	0.64	0.84	34	empty
3	494	0.60	0.74	41	empty
4	57	0.32	0.76	14	empty
5	55	0.27	0.73	10	empty

Compared structures

3I1Y · Crystal Structure of soluble epoxide Hydrolase · the same entry in another collection · chain A against A, TM-score 1.00
P34913 · AlphaFold monomer V2.0 prediction for bifunctional epoxide hydrolase 2 (P34913) · a predicted model of the same protein · chain A against A, TM-score 0.71

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 3I1Y · PDBe 3I1Y · UniProt P34913

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