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Human soluble epoxide hydrolase in complex with a cyclopropyl urea derivative

Analyse Human soluble epoxide hydrolase in complex with a cyclopropyl urea derivative in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4X6Y
Type: protein
Length: 632 residues
Chains: 2
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: S94
Pockets: 3 · best druggability 0.83

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Bifunctional epoxide hydrolase 2 (EC 3.3.2.10)	protein	316	44% helix, 16% strand	P34913

Ligands and binding sites

S94 · 4-phenoxy-N-[(1S,2R)-2-phenylcyclopropyl]piperidine-1-carboxamide · ligand · 2 copies · chains A, B

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

Pockets

3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	785	0.83	0.86	69	S94
2	753	0.83	0.85	61	S94
3	51	0.30	0.76	18	empty

Interfaces

1 interface between chains.

A–B · 760 Å² buried · 14 hydrogen bonds · protein-protein

Compared structures

4X6Y · Human soluble epoxide hydrolase in complex with a cyclopropyl urea derivative · 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 4X6Y · PDBe 4X6Y · UniProt P34913

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