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Chlorine in PDB 3wrz: N288Q-N321Q Mutant Beta-Lactamase Derived From Chromohalobacter Sp.560 (Without Soaking)

Enzymatic activity of N288Q-N321Q Mutant Beta-Lactamase Derived From Chromohalobacter Sp.560 (Without Soaking)

All present enzymatic activity of N288Q-N321Q Mutant Beta-Lactamase Derived From Chromohalobacter Sp.560 (Without Soaking):
3.5.2.6;

Protein crystallography data

The structure of N288Q-N321Q Mutant Beta-Lactamase Derived From Chromohalobacter Sp.560 (Without Soaking), PDB code: 3wrz 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) 29.12 / 1.80
Space group P 31
Cell size a, b, c (Å), α, β, γ (°) 114.928, 114.928, 67.567, 90.00, 90.00, 120.00
R / Rfree (%) 17.2 / 22.1

Other elements in 3wrz:

The structure of N288Q-N321Q Mutant Beta-Lactamase Derived From Chromohalobacter Sp.560 (Without Soaking) also contains other interesting chemical elements:

Calcium (Ca) 11 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the N288Q-N321Q Mutant Beta-Lactamase Derived From Chromohalobacter Sp.560 (Without Soaking) (pdb code 3wrz). 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 (Without Soaking), PDB code: 3wrz:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in 3wrz

Go back to Chlorine Binding Sites List in 3wrz
Chlorine binding site 1 out of 3 in the N288Q-N321Q Mutant Beta-Lactamase Derived From Chromohalobacter Sp.560 (Without Soaking)


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 (Without Soaking) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl406

b:20.3
occ:1.00
O A:HOH701 3.1 26.4 1.0
O A:HOH565 3.2 19.7 1.0
N A:VAL122 3.3 13.4 1.0
ND2 A:ASN153 3.4 12.1 1.0
CG2 A:VAL122 3.6 13.6 1.0
CB A:VAL122 3.9 14.2 1.0
CA A:PHE121 3.9 12.8 1.0
CD1 A:PHE121 3.9 13.8 1.0
CB A:ASN153 4.0 10.2 1.0
C A:PHE121 4.1 13.4 1.0
CG A:ASN153 4.2 10.9 1.0
CE2 A:TYR223 4.2 14.4 1.0
CA A:VAL122 4.2 14.3 1.0
CB A:PHE121 4.3 13.3 1.0
CG A:PHE121 4.6 13.8 1.0
O A:LEU120 4.7 11.2 1.0
O A:VAL122 4.8 15.2 1.0
OH A:TYR223 4.9 16.0 1.0
O A:HOH712 4.9 31.3 1.0
CD2 A:TYR223 4.9 13.5 1.0
CE1 A:PHE121 4.9 13.7 1.0
CZ A:TYR223 5.0 14.5 1.0

Chlorine binding site 2 out of 3 in 3wrz

Go back to Chlorine Binding Sites List in 3wrz
Chlorine binding site 2 out of 3 in the N288Q-N321Q Mutant Beta-Lactamase Derived From Chromohalobacter Sp.560 (Without Soaking)


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 (Without Soaking) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl403

b:27.1
occ:1.00
ND2 B:ASN153 3.3 19.0 1.0
O B:HOH601 3.4 19.1 1.0
N B:VAL122 3.5 19.6 1.0
CG2 B:VAL122 3.8 20.2 1.0
CD1 B:PHE121 4.0 19.6 1.0
CB B:VAL122 4.0 21.4 1.0
CB B:ASN153 4.0 16.1 1.0
CA B:PHE121 4.1 18.3 1.0
CG B:ASN153 4.1 16.8 1.0
CE2 B:TYR223 4.3 17.9 1.0
C B:PHE121 4.3 19.1 1.0
CA B:VAL122 4.3 21.5 1.0
CB B:PHE121 4.4 19.3 1.0
CG B:PHE121 4.7 19.6 1.0
O B:LEU120 4.8 16.5 1.0
O B:VAL122 4.8 23.5 1.0
CE1 B:PHE121 4.9 19.7 1.0
CD2 B:TYR223 5.0 17.3 1.0
OH B:TYR223 5.0 19.4 1.0

Chlorine binding site 3 out of 3 in 3wrz

Go back to Chlorine Binding Sites List in 3wrz
Chlorine binding site 3 out of 3 in the N288Q-N321Q Mutant Beta-Lactamase Derived From Chromohalobacter Sp.560 (Without Soaking)


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 (Without Soaking) within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cl405

b:18.0
occ:1.00
N C:VAL122 3.3 11.4 1.0
ND2 C:ASN153 3.4 12.1 1.0
O C:HOH582 3.5 14.5 1.0
CG2 C:VAL122 3.7 11.8 1.0
CA C:PHE121 3.9 11.0 1.0
CD1 C:PHE121 3.9 11.5 1.0
CB C:VAL122 3.9 12.2 1.0
CB C:ASN153 4.0 9.8 1.0
C C:PHE121 4.1 11.2 1.0
CG C:ASN153 4.1 10.6 1.0
CA C:VAL122 4.2 12.2 1.0
CB C:PHE121 4.2 11.3 1.0
CE2 C:TYR223 4.3 13.9 1.0
CG C:PHE121 4.6 11.4 1.0
O C:LEU120 4.6 10.2 1.0
O C:VAL122 4.8 13.1 1.0
CE1 C:PHE121 4.8 11.4 1.0
OH C:TYR223 4.9 15.1 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: Sat Dec 12 10:19:48 2020

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