Chlorine in PDB 3koo: Crystal Structure of Soluble Epoxide Hydrolase

All present enzymatic activity of Crystal Structure of Soluble Epoxide Hydrolase:
3.3.2.10;

The structure of Crystal Structure of Soluble Epoxide Hydrolase, PDB code: 3koo was solved by N.A.Farrow, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.20 / 2.79
Space group	P 65 2 2
Cell size a, b, c (Å), α, β, γ (°)	91.765, 91.765, 242.516, 90.00, 90.00, 120.00
R / Rfree (%)	21.3 / 30.7

The binding sites of Chlorine atom in the Crystal Structure of Soluble Epoxide Hydrolase (pdb code 3koo). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structure of Soluble Epoxide Hydrolase, PDB code: 3koo:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Crystal Structure of Soluble Epoxide Hydrolase


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Soluble Epoxide Hydrolase within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl556 b:88.8 occ:1.00 CL1 A:24D556 0.0 88.8 1.0 C2 A:24D556 1.8 80.6 1.0 C3 A:24D556 2.7 75.4 1.0 C25 A:24D556 2.7 79.0 1.0 CE1 A:PHE497 3.6 82.8 1.0 CB A:HIS524 3.7 69.2 1.0 CD1 A:PHE497 3.7 80.4 1.0 CG A:HIS524 3.8 72.1 1.0 CE A:MET419 3.9 78.8 1.0 C4 A:24D556 4.0 78.0 1.0 C23 A:24D556 4.0 76.8 1.0 CD2 A:HIS524 4.2 70.2 1.0 OD1 A:ASP496 4.3 66.3 1.0 CG2 A:VAL498 4.3 76.6 1.0 ND1 A:HIS524 4.3 67.5 1.0 CB A:VAL498 4.5 74.2 1.0 C5 A:24D556 4.6 72.8 1.0 SD A:MET419 4.8 72.1 1.0 CZ A:PHE497 4.8 84.7 1.0 NE2 A:HIS524 4.9 69.9 1.0 CE1 A:HIS524 4.9 67.9 1.0 N A:VAL498 5.0 71.3 1.0

Chlorine binding site 2 out of 2 in the Crystal Structure of Soluble Epoxide Hydrolase


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of Soluble Epoxide Hydrolase within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl556 b:86.3 occ:1.00 CL24 A:24D556 0.0 86.3 1.0 C23 A:24D556 1.7 76.8 1.0 C5 A:24D556 2.6 72.8 1.0 C25 A:24D556 2.8 79.0 1.0 C6 A:24D556 2.8 67.1 1.0 CD1 A:PHE267 3.5 73.0 1.0 O A:PHE267 3.7 71.4 1.0 CE1 A:PHE267 3.7 71.2 1.0 C4 A:24D556 3.9 78.0 1.0 C2 A:24D556 4.0 80.6 1.0 OH A:TYR466 4.1 71.8 1.0 N7 A:24D556 4.3 69.0 1.0 CH2 A:TRP525 4.4 63.1 1.0 C3 A:24D556 4.5 75.4 1.0 C A:PHE267 4.5 68.4 1.0 CD A:PRO268 4.7 66.5 1.0 CG A:PHE267 4.7 65.4 1.0 CZ2 A:TRP525 4.8 62.2 1.0 OD1 A:ASP335 4.9 65.8 1.0 O9 A:24D556 4.9 67.5 1.0

A.B.Eldrup, F.Soleymanzadeh, N.A.Farrow, A.Kukulka, S.De Lombaert. Optimization of Piperidyl-Ureas As Inhibitors of Soluble Epoxide Hydrolase. Bioorg.Med.Chem.Lett. V. 20 571 2010.
ISSN: ISSN 0960-894X
PubMed: 19969453
DOI: 10.1016/J.BMCL.2009.11.091