Chlorine in PDB 3ws4: N288Q-N321Q Mutant Beta-Lactamase Derived From Chromohalobacter Sp.560 (Condition-2A)

All present enzymatic activity of N288Q-N321Q Mutant Beta-Lactamase Derived From Chromohalobacter Sp.560 (Condition-2A):
3.5.2.6;

The structure of N288Q-N321Q Mutant Beta-Lactamase Derived From Chromohalobacter Sp.560 (Condition-2A), PDB code: 3ws4 was solved by S.Arai, Y.Yonezawa, N.Okazaki, F.Matsumoto, R.Shimizu, M.Yamada, M.Adachi, T.Tamada, H.Tokunaga, M.Ishibashi, M.Tokunaga, R.Kuroki, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	28.02 / 1.90
Space group	P 31
Cell size a, b, c (Å), α, β, γ (°)	115.019, 115.019, 67.800, 90.00, 90.00, 120.00
R / Rfree (%)	18.2 / 21.6

The structure of N288Q-N321Q Mutant Beta-Lactamase Derived From Chromohalobacter Sp.560 (Condition-2A) also contains other interesting chemical elements:

Strontium

(Sr)

8 atoms

The binding sites of Chlorine atom in the N288Q-N321Q Mutant Beta-Lactamase Derived From Chromohalobacter Sp.560 (Condition-2A) (pdb code 3ws4). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the N288Q-N321Q Mutant Beta-Lactamase Derived From Chromohalobacter Sp.560 (Condition-2A), PDB code: 3ws4:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in the N288Q-N321Q Mutant Beta-Lactamase Derived From Chromohalobacter Sp.560 (Condition-2A)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of N288Q-N321Q Mutant Beta-Lactamase Derived From Chromohalobacter Sp.560 (Condition-2A) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl404 b:39.2 occ:1.00 O A:HOH539 3.0 27.1 1.0 N A:VAL122 3.2 24.6 1.0 CG2 A:VAL122 3.7 26.4 1.0 ND2 A:ASN153 3.8 28.3 1.0 CB A:VAL122 3.8 25.8 1.0 CA A:PHE121 3.9 22.2 1.0 CD1 A:PHE121 4.0 23.0 1.0 C A:PHE121 4.0 24.9 1.0 CA A:VAL122 4.1 26.4 1.0 CB A:ASN153 4.2 21.8 1.0 CB A:PHE121 4.3 23.7 1.0 CG A:ASN153 4.4 23.1 1.0 CE2 A:TYR223 4.5 35.9 1.0 O A:VAL122 4.6 27.5 1.0 CG A:PHE121 4.6 23.4 1.0 O A:LEU120 4.7 23.3 1.0 C A:VAL122 4.9 26.8 1.0 CE1 A:PHE121 4.9 22.2 1.0

Chlorine binding site 2 out of 3 in the N288Q-N321Q Mutant Beta-Lactamase Derived From Chromohalobacter Sp.560 (Condition-2A)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of N288Q-N321Q Mutant Beta-Lactamase Derived From Chromohalobacter Sp.560 (Condition-2A) within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl403 b:39.7 occ:1.00 O B:HOH561 3.2 34.4 1.0 N B:VAL122 3.3 28.4 1.0 ND2 B:ASN153 3.6 26.3 1.0 CG2 B:VAL122 3.7 31.6 1.0 CB B:VAL122 3.9 31.0 1.0 CA B:PHE121 4.0 25.6 1.0 CD1 B:PHE121 4.0 24.8 1.0 CB B:ASN153 4.1 25.4 1.0 C B:PHE121 4.2 26.9 1.0 CA B:VAL122 4.2 30.9 1.0 CG B:ASN153 4.2 27.9 1.0 CB B:PHE121 4.4 24.8 1.0 CE2 B:TYR223 4.4 27.9 1.0 O B:LEU120 4.7 25.5 1.0 CG B:PHE121 4.7 24.9 1.0 O B:VAL122 4.8 34.7 1.0 CE1 B:PHE121 4.9 27.6 1.0

Chlorine binding site 3 out of 3 in the N288Q-N321Q Mutant Beta-Lactamase Derived From Chromohalobacter Sp.560 (Condition-2A)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of N288Q-N321Q Mutant Beta-Lactamase Derived From Chromohalobacter Sp.560 (Condition-2A) within 5.0Å range: probe atom residue distance (Å) B Occ C:Cl404 b:32.2 occ:1.00 O C:HOH562 2.9 28.4 1.0 N C:VAL122 3.2 24.4 1.0 ND2 C:ASN153 3.7 29.6 1.0 CG2 C:VAL122 3.7 25.0 1.0 CA C:PHE121 3.8 23.7 1.0 CB C:VAL122 3.9 25.2 1.0 CD1 C:PHE121 3.9 27.4 1.0 C C:PHE121 4.0 23.5 1.0 CB C:ASN153 4.1 22.4 1.0 CA C:VAL122 4.1 26.0 1.0 CB C:PHE121 4.2 24.3 1.0 CG C:ASN153 4.3 23.8 1.0 CE2 C:TYR223 4.5 31.5 1.0 CG C:PHE121 4.6 27.0 1.0 O C:LEU120 4.6 22.3 1.0 O C:VAL122 4.8 25.5 1.0 CE1 C:PHE121 4.9 26.8 1.0

S.Arai, Y.Yonezawa, N.Okazaki, F.Matsumoto, C.Shibazaki, R.Shimizu, M.Yamada, M.Adachi, T.Tamada, T.Kawamoto, H.Tokunaga, M.Ishibashi, M.Blaber, M.Tokunaga, R.Kuroki. Crystal Structure of Highly Acidic Beta-Lactamase From Moderate Halophile Chromohalobacter Sp. 560 and the Discovery of A Cs+ Selective Binding Site To Be Published.