MolNFT v2 · #218284 · protein

Comparison of room-temperature and cryogenic structures of soluble Epoxide Hydrolase with ligands bound.

8QWI · Bifunctional epoxide hydrolase 2: “Comparison of room-temperature and cryogenic structures of soluble Epoxide Hydrolase with ligands bound.”. X-ray diffraction at 2.12, 2 ligands (6N4, SO4), 6 pockets (best druggability 0.79).…

PDB: 8QWI
Type: protein
Length: 546 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.12
Source: Homo sapiens
Molecule: Bifunctional epoxide hydrolase 2
UniProt: P34913
Ligands: 6N4, SO4
Pockets: 6 · best druggability 0.79

Structure

x-ray diffraction · resolution 2.12 · 1 distinct chain · 47% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Bifunctional epoxide hydrolase 2	protein	546	47% helix, 14% strand	P34913

Ligands and binding sites

6N4 · 2-(1H-benzimidazol-2-ylsulfanyl)ethanol · ligand · chains A
SO4 · Sulfate ion · ion · chains A

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

Pockets

6 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	469	0.79	0.86	48	SO4, 6N4
2	280	0.64	0.81	34	empty
3	375	0.55	0.74	37	empty
4	60	0.46	0.84	19	empty
5	50	0.28	0.75	14	empty

Compared structures

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 8QWI · PDBe 8QWI · UniProt P34913

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