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Crystal structure of human bifunctional epoxide hydroxylase 2 complexed with A8

Analyse Crystal structure of human bifunctional epoxide hydroxylase 2 complexed with A8 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4C4Z
Type: protein
Length: 636 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, 3.1.3.76
UniProt: P34913
Ligands: W9L
Pockets: 2 · best druggability 0.84

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Bifunctional epoxide hydrolase 2 (EC 3.3.2.10, 3.1.3.76)	protein	318	41% helix, 16% strand	P34913

Ligands and binding sites

W9L · 1-ethyl-3-naphthalen-1-ylurea · ligand · 2 copies · chains A, B

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

Pockets

2 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	629	0.84	0.88	55	W9L
2	623	0.82	0.86	51	W9L

Interfaces

1 interface between chains.

A–B · 791 Å² buried · 17 hydrogen bonds · protein-protein

Compared structures

4C4Z · Crystal structure of human bifunctional epoxide hydroxylase 2 complexed with A8 · the same entry in another collection · chain B against B, 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 4C4Z · PDBe 4C4Z · UniProt P34913

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