Chlorine in PDB 2no4: Crystal Structure Analysis of A Dehalogenase

All present enzymatic activity of Crystal Structure Analysis of A Dehalogenase:
3.8.1.2;

The structure of Crystal Structure Analysis of A Dehalogenase, PDB code: 2no4 was solved by J.W.Schmidberger, M.C.J.Wilce, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	28.28 / 1.93
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	103.999, 103.999, 134.811, 90.00, 90.00, 120.00
R / Rfree (%)	18.4 / 21.6

The binding sites of Chlorine atom in the Crystal Structure Analysis of A Dehalogenase (pdb code 2no4). 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 Analysis of A Dehalogenase, PDB code: 2no4:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Crystal Structure Analysis of A Dehalogenase


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure Analysis of A Dehalogenase within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1013 b:69.7 occ:1.00 O A:HOH1054 2.6 53.0 1.0 O A:HOH1062 3.3 35.0 1.0 OE1 A:GLN198 3.4 36.3 0.4 OH A:TYR98 3.5 28.1 1.0 CE1 A:HIS20 3.6 41.3 1.0 O A:HOH1058 3.8 48.9 1.0 NE2 A:GLN198 3.8 37.4 0.6 CD A:ARG197 3.8 24.4 1.0 CB A:ARG197 4.1 26.4 1.0 ND1 A:HIS20 4.1 41.8 1.0 CD A:GLN198 4.1 34.9 0.4 CG A:GLN198 4.2 34.1 0.6 CE1 A:TYR98 4.3 27.6 1.0 CZ A:TYR98 4.3 27.7 1.0 CG A:GLN198 4.4 33.4 0.4 CG A:ARG197 4.5 24.0 1.0 CD A:GLN198 4.6 37.0 0.6 NE2 A:HIS20 4.7 42.5 1.0 O A:HOH1207 4.8 30.4 1.0 O A:HOH1067 4.9 37.7 1.0 O A:HOH1064 5.0 40.2 1.0

Chlorine binding site 2 out of 2 in the Crystal Structure Analysis of A Dehalogenase


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure Analysis of A Dehalogenase within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl1014 b:53.2 occ:1.00 O B:HOH1193 2.1 45.9 1.0 O B:HOH1159 2.6 49.0 1.0 O B:HOH1091 2.7 35.7 1.0 NE2 B:GLN198 3.5 37.0 0.6 NE2 B:GLN198 3.6 27.7 0.4 OH B:TYR98 3.9 27.7 1.0 CE1 B:HIS20 3.9 40.3 1.0 CG B:GLN198 4.0 26.4 0.4 CB B:ARG197 4.1 25.1 1.0 CD B:ARG197 4.1 25.4 1.0 CD B:GLN198 4.1 33.8 0.6 O B:HOH1107 4.2 31.5 1.0 CG B:GLN198 4.2 31.3 0.6 O B:HOH1217 4.3 37.7 1.0 O B:HOH1256 4.3 27.6 1.0 CD B:GLN198 4.4 27.1 0.4 ND1 B:HIS20 4.5 40.0 1.0 CG B:ARG197 4.6 25.9 1.0 CZ B:TYR98 4.7 25.3 1.0 CE1 B:TYR98 4.7 24.5 1.0 NE2 B:HIS20 4.9 40.7 1.0 O B:HOH1163 5.0 42.9 1.0 OE1 B:GLN198 5.0 36.9 0.6 NH1 B:ARG197 5.0 25.2 1.0

J.W.Schmidberger, J.A.Wilce, J.S.H.Tsang, M.C.J.Wilce. Crystal Structures of the Substrate Free-Enzyme, and Reaction Intermediate of the Had Superfamily Member, Haloacid Dehalogenase Dehiva From Burkholderia Cepacia MBA4 J.Mol.Biol. V. 368 706 2007.
ISSN: ISSN 0022-2836
PubMed: 17368477
DOI: 10.1016/J.JMB.2007.02.015