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Chlorine in PDB 2wgv: Crystal Structure of the Oxa-10 V117T Mutant at pH 6.5 Inhibited By A Chloride Ion

Enzymatic activity of Crystal Structure of the Oxa-10 V117T Mutant at pH 6.5 Inhibited By A Chloride Ion

All present enzymatic activity of Crystal Structure of the Oxa-10 V117T Mutant at pH 6.5 Inhibited By A Chloride Ion:
3.5.2.6;

Protein crystallography data

The structure of Crystal Structure of the Oxa-10 V117T Mutant at pH 6.5 Inhibited By A Chloride Ion, PDB code: 2wgv was solved by L.Vercheval, F.Kerff, C.Bauvois, E.Sauvage, R.Guiet, P.Charlier, M.Galleni, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 47.19 / 1.80
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 48.750, 101.700, 126.600, 90.00, 90.00, 90.00
R / Rfree (%) 18.212 / 20.909

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of the Oxa-10 V117T Mutant at pH 6.5 Inhibited By A Chloride Ion (pdb code 2wgv). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 5 binding sites of Chlorine where determined in the Crystal Structure of the Oxa-10 V117T Mutant at pH 6.5 Inhibited By A Chloride Ion, PDB code: 2wgv:
Jump to Chlorine binding site number: 1; 2; 3; 4; 5;

Chlorine binding site 1 out of 5 in 2wgv

Go back to Chlorine Binding Sites List in 2wgv
Chlorine binding site 1 out of 5 in the Crystal Structure of the Oxa-10 V117T Mutant at pH 6.5 Inhibited By A Chloride Ion


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of the Oxa-10 V117T Mutant at pH 6.5 Inhibited By A Chloride Ion within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl1268

b:22.3
occ:1.00
 O A:HOH2053 2.5 16.9 1.0
NE1 A:TRP154 3.1 15.4 1.0
NZ A:LYS70 3.2 17.2 1.0
CE A:LYS70 3.6 15.5 1.0
CG A:LYS70 3.7 15.9 1.0
CE2 A:TRP154 3.8 15.0 1.0
CZ2 A:TRP154 3.9 17.0 1.0
CB A:PHE120 3.9 14.6 1.0
OG A:SER67 3.9 18.9 1.0
OG1 A:THR117 3.9 15.4 1.0
CG2 A:THR117 4.0 14.9 1.0
CA A:THR117 4.1 15.1 1.0
CB A:THR117 4.2 15.6 1.0
CD1 A:TRP154 4.2 15.8 1.0
CD A:LYS70 4.3 15.4 1.0
O A:THR117 4.5 14.6 1.0
CA A:SER67 4.5 15.4 1.0
CG A:PHE120 4.6 15.8 1.0
CB A:SER67 4.6 16.4 1.0
CD2 A:LEU155 4.6 17.9 1.0
C A:THR117 4.8 15.4 1.0
CB A:LYS70 5.0 15.3 1.0
N A:THR117 5.0 14.8 1.0
N A:LYS70 5.0 14.6 1.0

Chlorine binding site 2 out of 5 in 2wgv

Go back to Chlorine Binding Sites List in 2wgv
Chlorine binding site 2 out of 5 in the Crystal Structure of the Oxa-10 V117T Mutant at pH 6.5 Inhibited By A Chloride Ion


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of the Oxa-10 V117T Mutant at pH 6.5 Inhibited By A Chloride Ion within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl1269

b:30.2
occ:1.00
 N A:ALA98 3.4 23.2 1.0
CB A:ALA98 3.7 23.6 1.0
CG A:PRO118 3.9 17.5 1.0
CZ3 A:TRP102 4.0 16.9 1.0
CD A:PRO118 4.1 15.9 1.0
CA A:ARG97 4.1 21.7 1.0
CB A:PRO118 4.1 17.1 1.0
CA A:ALA98 4.2 23.5 1.0
CE3 A:TRP102 4.2 17.4 1.0
C A:ARG97 4.2 21.9 1.0
CB A:ARG97 4.3 21.3 1.0
CG A:ARG97 4.6 20.7 1.0

Chlorine binding site 3 out of 5 in 2wgv

Go back to Chlorine Binding Sites List in 2wgv
Chlorine binding site 3 out of 5 in the Crystal Structure of the Oxa-10 V117T Mutant at pH 6.5 Inhibited By A Chloride Ion


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Crystal Structure of the Oxa-10 V117T Mutant at pH 6.5 Inhibited By A Chloride Ion within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl1270

b:35.7
occ:1.00
 O A:HOH2215 2.4 32.4 1.0
NE A:ARG250 3.3 17.8 1.0
O A:HOH2093 3.6 51.5 1.0
CD A:LYS251 3.7 20.1 1.0
NH2 A:ARG250 3.8 18.5 1.0
CG A:LYS251 3.9 19.7 1.0
CA A:PRO248 3.9 19.3 1.0
CZ A:ARG250 4.0 17.8 1.0
CG A:ARG250 4.0 19.8 1.0
O A:LEU247 4.1 19.8 1.0
CE A:LYS251 4.2 21.6 1.0
CD A:ARG250 4.3 20.1 1.0
CB A:LYS251 4.4 20.1 1.0
O A:PRO248 4.5 19.6 1.0
N A:PRO248 4.5 19.4 1.0
C A:LEU247 4.6 19.6 1.0
O A:HOH2216 4.6 29.4 1.0
C A:PRO248 4.6 19.4 1.0
NZ A:LYS251 4.7 19.9 1.0
CB A:PRO248 4.8 19.0 1.0
N A:LYS251 4.9 19.9 1.0
CG2 A:THR206 5.0 16.5 1.0

Chlorine binding site 4 out of 5 in 2wgv

Go back to Chlorine Binding Sites List in 2wgv
Chlorine binding site 4 out of 5 in the Crystal Structure of the Oxa-10 V117T Mutant at pH 6.5 Inhibited By A Chloride Ion


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Crystal Structure of the Oxa-10 V117T Mutant at pH 6.5 Inhibited By A Chloride Ion within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl1271

b:36.3
occ:1.00
 CB A:LYS152 3.6 19.6 1.0
CG A:GLU156 3.7 18.6 1.0
CB A:LEU155 3.9 15.2 1.0
CD1 A:LEU155 4.0 17.8 1.0
CD A:GLU156 4.1 22.9 1.0
OE2 A:GLU156 4.2 22.1 1.0
CD A:LYS152 4.3 25.8 1.0
CB A:GLU156 4.4 16.9 1.0
NE2 A:GLN121 4.4 13.8 1.0
CG A:LYS152 4.5 21.9 1.0
CG A:LEU155 4.6 16.3 1.0
CA A:LYS152 4.7 19.1 1.0
N A:GLU156 4.8 15.8 1.0
OE1 A:GLU156 4.8 27.9 1.0
O A:LYS152 5.0 16.8 1.0
C A:LEU155 5.0 16.0 1.0

Chlorine binding site 5 out of 5 in 2wgv

Go back to Chlorine Binding Sites List in 2wgv
Chlorine binding site 5 out of 5 in the Crystal Structure of the Oxa-10 V117T Mutant at pH 6.5 Inhibited By A Chloride Ion


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 5 of Crystal Structure of the Oxa-10 V117T Mutant at pH 6.5 Inhibited By A Chloride Ion within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl1266

b:41.3
occ:1.00
 O B:HOH2030 2.7 32.1 1.0
NE1 B:TRP154 3.1 24.4 1.0
NZ B:LYS70 3.2 24.2 1.0
CG B:LYS70 3.6 23.6 1.0
CE B:LYS70 3.7 24.7 1.0
CE2 B:TRP154 3.8 23.9 1.0
CZ2 B:TRP154 3.9 23.1 1.0
CB B:PHE120 3.9 13.9 1.0
OG1 B:THR117 4.1 18.4 1.0
CG2 B:THR117 4.1 17.5 1.0
CD1 B:TRP154 4.2 24.6 1.0
CA B:THR117 4.2 18.5 1.0
CD B:LYS70 4.3 22.9 1.0
OG B:SER67 4.3 25.7 1.0
CB B:THR117 4.4 18.6 1.0
CA B:SER67 4.5 23.9 1.0
CG B:PHE120 4.5 14.6 1.0
O B:THR117 4.6 18.1 1.0
CD2 B:LEU155 4.8 26.6 1.0
N B:LYS70 4.8 23.0 1.0
CB B:SER67 4.9 23.7 1.0
CB B:LYS70 4.9 23.5 1.0
O B:ALA66 4.9 24.1 1.0
C B:THR117 5.0 18.1 1.0
CD2 B:PHE120 5.0 15.0 1.0

Reference:

L.Vercheval, C.Bauvois, A.Di Paolo, F.Borel, J.L.Ferrer, E.Sauvage, A.Matagne, J.M.Frere, P.Charlier, M.Galleni, F.Kerff. Three Factors That Modulate the Activity of Class D Beta-Lactamases and Interfere with the Post- Translational Carboxylation of LYS70. Biochem.J. V. 432 495 2010.
ISSN: ISSN 0264-6021
PubMed: 21108605
DOI: 10.1042/BJ20101122
Page generated: Fri Jul 11 01:22:57 2025

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