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Chlorine in PDB 3ws0: N288Q-N321Q Mutant Beta-Lactamase Derived From Chromohalobacter Sp.560 (Condition-1A)

Enzymatic activity of N288Q-N321Q Mutant Beta-Lactamase Derived From Chromohalobacter Sp.560 (Condition-1A)

All present enzymatic activity of N288Q-N321Q Mutant Beta-Lactamase Derived From Chromohalobacter Sp.560 (Condition-1A):
3.5.2.6;

Protein crystallography data

The structure of N288Q-N321Q Mutant Beta-Lactamase Derived From Chromohalobacter Sp.560 (Condition-1A), PDB code: 3ws0 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) 29.88 / 2.00
Space group P 31
Cell size a, b, c (Å), α, β, γ (°) 115.393, 115.393, 67.652, 90.00, 90.00, 120.00
R / Rfree (%) 19 / 22.4

Other elements in 3ws0:

The structure of N288Q-N321Q Mutant Beta-Lactamase Derived From Chromohalobacter Sp.560 (Condition-1A) also contains other interesting chemical elements:

Caesium (Cs) 2 atoms
Calcium (Ca) 10 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the N288Q-N321Q Mutant Beta-Lactamase Derived From Chromohalobacter Sp.560 (Condition-1A) (pdb code 3ws0). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 4 binding sites of Chlorine where determined in the N288Q-N321Q Mutant Beta-Lactamase Derived From Chromohalobacter Sp.560 (Condition-1A), PDB code: 3ws0:
Jump to Chlorine binding site number: 1; 2; 3; 4;

Chlorine binding site 1 out of 4 in 3ws0

Go back to Chlorine Binding Sites List in 3ws0
Chlorine binding site 1 out of 4 in the N288Q-N321Q Mutant Beta-Lactamase Derived From Chromohalobacter Sp.560 (Condition-1A)


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-1A) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl406

b:33.2
occ:1.00
 O A:HOH547 3.2 24.5 1.0
N A:VAL122 3.2 20.1 1.0
CG2 A:VAL122 3.7 20.2 1.0
CA A:PHE121 3.8 19.4 1.0
ND2 A:ASN153 3.9 23.6 1.0
CD1 A:PHE121 3.9 21.4 1.0
CB A:VAL122 3.9 21.7 1.0
C A:PHE121 4.0 20.1 1.0
CB A:ASN153 4.1 18.2 1.0
CA A:VAL122 4.2 21.8 1.0
CB A:PHE121 4.2 21.4 1.0
CG A:ASN153 4.3 20.2 1.0
CE2 A:TYR223 4.4 24.8 1.0
CG A:PHE121 4.5 21.5 1.0
O A:LEU120 4.6 17.1 1.0
O A:VAL122 4.8 24.4 1.0
CE1 A:PHE121 4.9 21.2 1.0
N A:PHE121 5.0 19.0 1.0

Chlorine binding site 2 out of 4 in 3ws0

Go back to Chlorine Binding Sites List in 3ws0
Chlorine binding site 2 out of 4 in the N288Q-N321Q Mutant Beta-Lactamase Derived From Chromohalobacter Sp.560 (Condition-1A)


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-1A) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl404

b:42.4
occ:1.00
 N B:VAL122 3.3 31.7 1.0
CG2 B:VAL122 3.7 32.4 1.0
ND2 B:ASN153 3.8 26.1 1.0
CA B:PHE121 3.8 29.0 1.0
CD1 B:PHE121 3.9 28.2 1.0
CB B:ASN153 4.0 25.4 1.0
CB B:VAL122 4.0 33.9 1.0
C B:PHE121 4.0 30.6 1.0
CG B:ASN153 4.2 25.3 1.0
CA B:VAL122 4.2 33.7 1.0
CB B:PHE121 4.3 30.0 1.0
CE2 B:TYR223 4.4 28.8 1.0
O B:LEU120 4.5 26.0 1.0
CG B:PHE121 4.6 29.3 1.0
O B:VAL122 4.9 35.0 1.0
CE1 B:PHE121 4.9 27.6 1.0
N B:PHE121 5.0 28.4 1.0

Chlorine binding site 3 out of 4 in 3ws0

Go back to Chlorine Binding Sites List in 3ws0
Chlorine binding site 3 out of 4 in the N288Q-N321Q Mutant Beta-Lactamase Derived From Chromohalobacter Sp.560 (Condition-1A)


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-1A) within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cl405

b:26.8
occ:1.00
 N C:TYR190 3.2 20.2 1.0
NH1 C:ARG176 3.4 36.5 1.0
N C:ASP191 3.5 24.4 1.0
CB C:TYR190 3.9 20.4 1.0
CA C:TYR190 3.9 20.6 1.0
O C:ASP191 4.0 25.5 1.0
CE3 C:TRP189 4.1 27.4 1.0
CA C:TRP189 4.1 21.4 1.0
C C:TRP189 4.1 20.6 1.0
C C:TYR190 4.2 22.4 1.0
CG2 C:VAL172 4.4 26.9 1.0
CD2 C:TYR190 4.4 20.1 1.0
CA C:ASP191 4.4 27.5 1.0
CZ C:ARG176 4.5 37.0 1.0
CB C:ASP191 4.5 31.0 1.0
CB C:TRP189 4.6 23.2 1.0
C C:ASP191 4.6 26.7 1.0
CG C:TYR190 4.7 19.6 1.0
NE C:ARG176 4.7 36.6 1.0
CZ3 C:TRP189 4.8 29.6 1.0
OD2 C:ASP191 4.9 34.8 1.0
CD2 C:TRP189 5.0 26.2 1.0

Chlorine binding site 4 out of 4 in 3ws0

Go back to Chlorine Binding Sites List in 3ws0
Chlorine binding site 4 out of 4 in the N288Q-N321Q Mutant Beta-Lactamase Derived From Chromohalobacter Sp.560 (Condition-1A)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of N288Q-N321Q Mutant Beta-Lactamase Derived From Chromohalobacter Sp.560 (Condition-1A) within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cl406

b:29.8
occ:1.00
 N C:VAL122 3.3 18.1 1.0
O C:HOH561 3.4 25.3 1.0
ND2 C:ASN153 3.7 22.0 1.0
CG2 C:VAL122 3.7 19.0 1.0
CA C:PHE121 3.8 16.8 1.0
CB C:ASN153 3.9 16.6 1.0
CD1 C:PHE121 3.9 20.0 1.0
CB C:VAL122 4.0 19.4 1.0
C C:PHE121 4.0 17.2 1.0
CG C:ASN153 4.2 18.4 1.0
CA C:VAL122 4.2 19.1 1.0
CB C:PHE121 4.3 18.4 1.0
CE2 C:TYR223 4.4 25.5 1.0
O C:LEU120 4.5 14.4 1.0
CG C:PHE121 4.6 19.6 1.0
O C:VAL122 4.9 21.8 1.0
CE1 C:PHE121 4.9 20.8 1.0
N C:PHE121 5.0 16.4 1.0
CD2 C:TYR223 5.0 24.7 1.0

Reference:

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.
Page generated: Fri Jul 11 12:03:04 2025

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