MolNFT v1 · #113649 · protein

Ligand complex structure of soluble epoxide hydrolase

5ALR · Bifunctional epoxide hydrolase 2: “Ligand complex structure of soluble epoxide hydrolase”. X-ray diffraction, 2 ligands (8TM, SO4), 4 pockets (best druggability 0.82). MolNFT v1 #113649 on GenesisL1: 3D structure, binding sites and…

PDB: 5ALR
Type: protein
Length: 542 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, 3.1.3.76
UniProt: P34913
Ligands: 8TM, SO4
Pockets: 4 · best druggability 0.82

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Bifunctional epoxide hydrolase 2 (EC 3.3.2.10, 3.1.3.76)	protein	542	45% helix, 15% strand	P34913

Ligands and binding sites

8TM · N-[4-(trifluoromethylsulfanyl)phenyl]quinazolin-4-amine · ligand · chains A
SO4 · Sulfate ion · ion · 3 copies · chains A

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

Pockets

4 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	615	0.82	0.86	52	SO4, 8TM
2	511	0.61	0.74	44	empty
3	184	0.59	0.82	30	empty
4	54	0.29	0.76	15	empty

Compared structures

5ALR · ligand complex structure of soluble epoxide hydrolase · 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 5ALR · PDBe 5ALR · UniProt P34913

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