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Chlorine in PDB 6ivv: Structure of Peptidyl-Trna Hydrolase From Acinetobacter Baumannii with Multiple Surface Binding Regions at 1.26A Resolution

Enzymatic activity of Structure of Peptidyl-Trna Hydrolase From Acinetobacter Baumannii with Multiple Surface Binding Regions at 1.26A Resolution

All present enzymatic activity of Structure of Peptidyl-Trna Hydrolase From Acinetobacter Baumannii with Multiple Surface Binding Regions at 1.26A Resolution:
3.1.1.29;

Protein crystallography data

The structure of Structure of Peptidyl-Trna Hydrolase From Acinetobacter Baumannii with Multiple Surface Binding Regions at 1.26A Resolution, PDB code: 6ivv was solved by V.Viswanathan, P.Sharma, A.Chaudhary, S.Sharma, T.P.Singh, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 49.77 / 1.26
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 33.945, 66.034, 75.711, 90.00, 90.00, 90.00
R / Rfree (%) 15.8 / 18.4

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Structure of Peptidyl-Trna Hydrolase From Acinetobacter Baumannii with Multiple Surface Binding Regions at 1.26A Resolution (pdb code 6ivv). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the Structure of Peptidyl-Trna Hydrolase From Acinetobacter Baumannii with Multiple Surface Binding Regions at 1.26A Resolution, PDB code: 6ivv:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in 6ivv

Go back to Chlorine Binding Sites List in 6ivv
Chlorine binding site 1 out of 3 in the Structure of Peptidyl-Trna Hydrolase From Acinetobacter Baumannii with Multiple Surface Binding Regions at 1.26A Resolution


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structure of Peptidyl-Trna Hydrolase From Acinetobacter Baumannii with Multiple Surface Binding Regions at 1.26A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl201

b:17.1
occ:0.90
 O A:HOH422 3.1 19.0 1.0
ND2 A:ASN12 3.3 11.5 1.0
ND2 A:ASN116 3.4 21.1 1.0
CD2 A:HIS22 3.4 10.5 1.0
O A:HOH495 3.5 41.2 1.0
CB A:MET69 3.6 10.8 1.0
NE2 A:HIS22 3.7 11.7 1.0
O A:HOH480 3.7 50.3 1.0
OD1 A:ASN12 4.1 11.4 1.0
CG A:ASN12 4.2 10.9 1.0
OD1 A:ASN116 4.2 16.8 1.0
CG A:ASN116 4.3 17.1 1.0
CG A:MET69 4.3 9.5 1.0
CD2 A:LEU150 4.4 16.6 1.0
CG A:HIS22 4.7 9.2 1.0
CA A:MET69 4.9 10.4 1.0
N A:MET69 4.9 11.3 1.0

Chlorine binding site 2 out of 3 in 6ivv

Go back to Chlorine Binding Sites List in 6ivv
Chlorine binding site 2 out of 3 in the Structure of Peptidyl-Trna Hydrolase From Acinetobacter Baumannii with Multiple Surface Binding Regions at 1.26A Resolution


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Structure of Peptidyl-Trna Hydrolase From Acinetobacter Baumannii with Multiple Surface Binding Regions at 1.26A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl202

b:23.7
occ:0.90
 NH1 A:ARG133 3.2 22.9 1.0
O A:HOH315 3.2 24.2 1.0
O A:HOH449 3.4 38.1 1.0
CD A:ARG105 3.7 26.4 1.0
CB A:LYS107 3.9 11.9 1.0
CB A:ARG105 3.9 14.3 1.0
CD A:ARG133 3.9 12.4 1.0
CZ A:ARG133 4.2 22.1 1.0
CD A:LYS107 4.3 18.1 1.0
CG A:LYS107 4.3 15.7 1.0
NH1 A:ARG105 4.3 43.5 1.0
CG A:ARG105 4.4 19.3 1.0
NE A:ARG133 4.5 16.0 1.0
CA A:LYS107 4.5 10.8 1.0
O A:LEU106 4.6 12.5 1.0
O A:HOH431 4.7 35.5 1.0
NE A:ARG105 4.9 33.5 1.0
N A:LYS107 4.9 9.8 1.0
C A:LEU106 5.0 10.1 1.0

Chlorine binding site 3 out of 3 in 6ivv

Go back to Chlorine Binding Sites List in 6ivv
Chlorine binding site 3 out of 3 in the Structure of Peptidyl-Trna Hydrolase From Acinetobacter Baumannii with Multiple Surface Binding Regions at 1.26A Resolution


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Structure of Peptidyl-Trna Hydrolase From Acinetobacter Baumannii with Multiple Surface Binding Regions at 1.26A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl203

b:20.8
occ:0.90
 O A:HOH447 2.9 40.2 1.0
NE2 A:HIS94 2.9 8.9 1.0
NH1 A:ARG131 3.1 9.6 1.0
CG A:ARG131 3.3 8.1 1.0
CB A:ARG131 3.4 7.8 1.0
CD A:ARG131 3.5 8.2 1.0
CE1 A:HIS94 3.5 8.4 1.0
CG A:ARG133 3.7 10.1 1.0
CD A:LYS107 3.8 18.1 1.0
CD1 A:LEU118 3.8 10.4 1.0
CD A:ARG133 3.8 12.4 1.0
NE A:ARG133 3.9 16.0 1.0
CD2 A:HIS94 4.1 8.5 1.0
CZ A:ARG131 4.1 9.3 1.0
NE A:ARG131 4.2 8.4 1.0
CE A:LYS107 4.3 23.7 1.0
O A:GLY111 4.4 15.5 1.0
CZ A:ARG133 4.6 22.1 1.0
OE1 A:GLU96 4.6 13.2 1.0
CG A:LYS107 4.7 15.7 1.0
ND1 A:HIS94 4.7 8.0 1.0
CB A:LYS107 4.8 11.9 1.0
CA A:ARG131 4.9 7.6 1.0

Reference:

T.P.Singh, V.Viswanathan. Structure of Peptide T-Rna Hydrolase From Acinetobacter Baumannii with Multiple Surface Binding Sites at 1.26 Angstrom Resolution. To Be Published.
Page generated: Sun Jul 28 01:52:50 2024

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