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Sodium in PDB 1qw7: Structure of An Engineered Organophosphorous Hydrolase with Increased Activity Toward Hydrolysis of Phosphothiolate Bonds

Enzymatic activity of Structure of An Engineered Organophosphorous Hydrolase with Increased Activity Toward Hydrolysis of Phosphothiolate Bonds

All present enzymatic activity of Structure of An Engineered Organophosphorous Hydrolase with Increased Activity Toward Hydrolysis of Phosphothiolate Bonds:
3.1.8.1;

Protein crystallography data

The structure of Structure of An Engineered Organophosphorous Hydrolase with Increased Activity Toward Hydrolysis of Phosphothiolate Bonds, PDB code: 1qw7 was solved by A.D.Mesecar, J.K.Grimsley, T.Holton, J.R.Wild, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 49.50 / 1.90
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 126.719, 89.879, 68.337, 90.00, 91.73, 90.00
R / Rfree (%) 17.9 / 23

Other elements in 1qw7:

The structure of Structure of An Engineered Organophosphorous Hydrolase with Increased Activity Toward Hydrolysis of Phosphothiolate Bonds also contains other interesting chemical elements:

Cobalt (Co) 4 atoms

Sodium Binding Sites:

The binding sites of Sodium atom in the Structure of An Engineered Organophosphorous Hydrolase with Increased Activity Toward Hydrolysis of Phosphothiolate Bonds (pdb code 1qw7). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total 2 binding sites of Sodium where determined in the Structure of An Engineered Organophosphorous Hydrolase with Increased Activity Toward Hydrolysis of Phosphothiolate Bonds, PDB code: 1qw7:
Jump to Sodium binding site number: 1; 2;

Sodium binding site 1 out of 2 in 1qw7

Go back to Sodium Binding Sites List in 1qw7
Sodium binding site 1 out of 2 in the Structure of An Engineered Organophosphorous Hydrolase with Increased Activity Toward Hydrolysis of Phosphothiolate Bonds


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Structure of An Engineered Organophosphorous Hydrolase with Increased Activity Toward Hydrolysis of Phosphothiolate Bonds within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na605

b:40.8
occ:1.00
OD1 A:ASN38 2.8 31.7 1.0
O A:HOH913 2.8 31.2 1.0
O A:ILE154 2.8 22.4 1.0
CG2 A:ILE154 3.6 18.6 1.0
C A:ILE154 3.7 23.8 1.0
CG A:ASN38 3.8 28.3 1.0
O A:HOH777 3.8 26.4 1.0
CD A:ARG164 4.1 33.4 1.0
ND2 A:ASN38 4.2 24.8 1.0
CB A:ARG164 4.3 22.4 1.0
CA A:GLN155 4.5 24.8 1.0
N A:GLN155 4.5 24.7 1.0
O A:HOH784 4.5 27.3 1.0
O A:HOH816 4.5 23.6 1.0
O A:ALA165 4.5 18.1 1.0
O A:HOH954 4.6 39.0 1.0
CG A:ARG164 4.6 23.4 1.0
CA A:ILE154 4.6 21.3 1.0
CB A:ILE154 4.7 18.4 1.0
CG2 A:VAL196 4.9 23.4 1.0

Sodium binding site 2 out of 2 in 1qw7

Go back to Sodium Binding Sites List in 1qw7
Sodium binding site 2 out of 2 in the Structure of An Engineered Organophosphorous Hydrolase with Increased Activity Toward Hydrolysis of Phosphothiolate Bonds


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 2 of Structure of An Engineered Organophosphorous Hydrolase with Increased Activity Toward Hydrolysis of Phosphothiolate Bonds within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Na606

b:41.2
occ:1.00
O B:HOH830 2.6 27.0 1.0
O B:ILE154 2.7 21.2 1.0
OD1 B:ASN38 2.7 30.5 1.0
O B:HOH802 2.8 27.6 1.0
CG2 B:ILE154 3.5 17.5 1.0
O B:HOH755 3.7 21.6 1.0
CG B:ASN38 3.7 28.9 1.0
C B:ILE154 3.7 21.3 1.0
ND2 B:ASN38 4.0 22.0 1.0
CD B:ARG164 4.1 23.3 1.0
O B:HOH798 4.4 29.0 1.0
CB B:ARG164 4.4 13.6 1.0
CA B:GLN155 4.5 21.4 1.0
O B:ALA165 4.5 16.6 1.0
N B:GLN155 4.5 21.9 1.0
O B:HOH906 4.5 38.0 1.0
CA B:ILE154 4.6 18.0 1.0
CB B:ILE154 4.7 17.7 1.0
CG B:ARG164 4.7 20.1 1.0
CG2 B:VAL196 4.8 21.4 1.0
O B:HOH737 5.0 21.6 1.0

Reference:

J.K.Grimsley, B.Calamini, J.R.Wild, A.D.Mesecar. Structural and Mutational Studies of Organophosphorus Hydrolase Reveal A Cryptic and Functional Allosteric-Binding Site. Arch.Biochem.Biophys. V. 442 169 2005.
ISSN: ISSN 0003-9861
PubMed: 16188223
DOI: 10.1016/J.ABB.2005.08.012
Page generated: Sun Oct 6 21:59:01 2024

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