Chlorine in PDB 3ws5: N288Q-N321Q Mutant Beta-Lactamase Derived From Chromohalobacter Sp.560 (Condition-2B)

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

The structure of N288Q-N321Q Mutant Beta-Lactamase Derived From Chromohalobacter Sp.560 (Condition-2B), PDB code: 3ws5 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)	29.59 / 2.80
Space group	P 31
Cell size a, b, c (Å), α, β, γ (°)	114.262, 114.262, 66.998, 90.00, 90.00, 120.00
R / Rfree (%)	17.6 / 20.7

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

Strontium	(Sr)	1 atom
Calcium	(Ca)	1 atom

The binding sites of Chlorine atom in the N288Q-N321Q Mutant Beta-Lactamase Derived From Chromohalobacter Sp.560 (Condition-2B) (pdb code 3ws5). 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-2B), PDB code: 3ws5:
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-2B)


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-2B) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl402 b:41.9 occ:1.00 N A:VAL122 3.5 26.0 1.0 CG2 A:VAL122 3.7 26.8 1.0 ND2 A:ASN153 3.7 32.1 1.0 CD1 A:PHE121 3.8 21.1 1.0 CA A:PHE121 3.9 22.5 1.0 CB A:PHE121 4.0 22.1 1.0 CB A:VAL122 4.1 26.7 1.0 CE2 A:TYR223 4.2 26.4 1.0 C A:PHE121 4.2 24.0 1.0 CA A:VAL122 4.4 26.0 1.0 CG A:PHE121 4.4 21.8 1.0 CB A:ASN153 4.4 27.4 1.0 CG A:ASN153 4.6 28.6 1.0 OH A:TYR223 4.7 26.4 1.0 CE1 A:PHE121 4.8 21.3 1.0 O A:VAL122 4.8 24.2 1.0 CZ A:TYR223 4.9 26.3 1.0 CD2 A:TYR223 5.0 25.8 1.0 O A:LEU120 5.0 23.4 1.0

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


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-2B) within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl402 b:48.3 occ:1.00 CG2 B:VAL122 3.4 43.7 1.0 N B:VAL122 3.4 40.2 1.0 ND2 B:ASN153 3.4 31.6 1.0 CB B:ASN153 3.9 33.7 1.0 CB B:VAL122 4.0 44.2 1.0 CA B:PHE121 4.0 36.2 1.0 CE2 B:TYR223 4.0 36.0 1.0 CG B:ASN153 4.1 31.5 1.0 CD1 B:PHE121 4.2 40.9 1.0 C B:PHE121 4.2 35.8 1.0 CA B:VAL122 4.3 44.2 1.0 CB B:PHE121 4.4 38.2 1.0 O B:LEU120 4.8 34.2 1.0 CD2 B:TYR223 4.8 38.8 1.0 CG B:PHE121 4.8 38.1 1.0 OH B:TYR223 4.8 36.8 1.0 CZ B:TYR223 4.9 36.0 1.0 O B:VAL217 4.9 41.5 1.0

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


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-2B) within 5.0Å range: probe atom residue distance (Å) B Occ C:Cl401 b:41.3 occ:1.00 N C:VAL122 3.3 32.8 1.0 ND2 C:ASN153 3.4 26.6 1.0 CG2 C:VAL122 3.5 32.7 1.0 CA C:PHE121 3.7 29.7 1.0 CD1 C:PHE121 3.8 37.1 1.0 CB C:ASN153 4.0 27.1 1.0 C C:PHE121 4.0 31.5 1.0 CB C:PHE121 4.0 30.9 1.0 CB C:VAL122 4.0 32.5 1.0 CE2 C:TYR223 4.1 31.6 1.0 CG C:ASN153 4.1 27.4 1.0 CA C:VAL122 4.2 32.8 1.0 CG C:PHE121 4.4 33.6 1.0 O C:LEU120 4.6 26.8 1.0 CE1 C:PHE121 4.8 35.6 1.0 OH C:TYR223 4.9 35.4 1.0 CD2 C:TYR223 4.9 30.4 1.0 N C:PHE121 4.9 28.4 1.0 CZ C:TYR223 4.9 33.6 1.0 O C:VAL122 5.0 33.8 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.