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Potassium in PDB 1usb: Rational Design of A Novel Enzyme - Efficient Thioester Hydrolysis Enabled By the Incorporation of A Single His Residue Into Human Glutathione Transferase A1-1
Enzymatic activity of Rational Design of A Novel Enzyme - Efficient Thioester Hydrolysis Enabled By the Incorporation of A Single His Residue Into Human Glutathione Transferase A1-1
All present enzymatic activity of Rational Design of A Novel Enzyme - Efficient Thioester Hydrolysis Enabled By the Incorporation of A Single His Residue Into Human Glutathione Transferase A1-1:
2.5.1.18;
2.5.1.18;
Protein crystallography data
The structure of Rational Design of A Novel Enzyme - Efficient Thioester Hydrolysis Enabled By the Incorporation of A Single His Residue Into Human Glutathione Transferase A1-1, PDB code: 1usb
was solved by
E.Jakobsson,
G.J.Kleywegt,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
| Resolution Low / High (Å) | 40.00 / 2.07 |
| Space group | C 1 2 1 |
| Cell size a, b, c (Å), α, β, γ (°) | 98.906, 92.050, 51.272, 90.00, 93.21, 90.00 |
| R / Rfree (%) | 18.9 / 24.5 |
Other elements in 1usb:
The structure of Rational Design of A Novel Enzyme - Efficient Thioester Hydrolysis Enabled By the Incorporation of A Single His Residue Into Human Glutathione Transferase A1-1 also contains other interesting chemical elements:
| Chlorine | (Cl) | 2 atoms |
Potassium Binding Sites:
The binding sites of Potassium atom in the Rational Design of A Novel Enzyme - Efficient Thioester Hydrolysis Enabled By the Incorporation of A Single His Residue Into Human Glutathione Transferase A1-1
(pdb code 1usb). This binding sites where shown within
5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Rational Design of A Novel Enzyme - Efficient Thioester Hydrolysis Enabled By the Incorporation of A Single His Residue Into Human Glutathione Transferase A1-1, PDB code: 1usb:
Jump to Potassium binding site number: 1; 2;
In total 2 binding sites of Potassium where determined in the Rational Design of A Novel Enzyme - Efficient Thioester Hydrolysis Enabled By the Incorporation of A Single His Residue Into Human Glutathione Transferase A1-1, PDB code: 1usb:
Jump to Potassium binding site number: 1; 2;
Potassium binding site 1 out of 2 in 1usb
Go back to
Potassium Binding Sites List in 1usb
Potassium binding site 1 out
of 2 in the Rational Design of A Novel Enzyme - Efficient Thioester Hydrolysis Enabled By the Incorporation of A Single His Residue Into Human Glutathione Transferase A1-1
Mono view
Stereo pair view
Mono view
Stereo pair view
A full contact list of Potassium with other atoms in the K binding
site number 1 of Rational Design of A Novel Enzyme - Efficient Thioester Hydrolysis Enabled By the Incorporation of A Single His Residue Into Human Glutathione Transferase A1-1 within 5.0Å range:
|
Potassium binding site 2 out of 2 in 1usb
Go back to
Potassium Binding Sites List in 1usb
Potassium binding site 2 out
of 2 in the Rational Design of A Novel Enzyme - Efficient Thioester Hydrolysis Enabled By the Incorporation of A Single His Residue Into Human Glutathione Transferase A1-1
Mono view
Stereo pair view
Mono view
Stereo pair view
A full contact list of Potassium with other atoms in the K binding
site number 2 of Rational Design of A Novel Enzyme - Efficient Thioester Hydrolysis Enabled By the Incorporation of A Single His Residue Into Human Glutathione Transferase A1-1 within 5.0Å range:
|
Reference:
S.Hederos,
K.S.Broo,
E.Jakobsson,
G.J.Kleywegt,
B.Mannervik,
L.Baltzer.
Incorporation of A Single His Residue By Rational Design Enables Thiol-Ester Hydrolysis By Human Glutathione Transferase A1-1 Proc.Natl.Acad.Sci.Usa V. 101 13163 2004.
ISSN: ISSN 0027-8424
PubMed: 15333749
DOI: 10.1073/PNAS.0403045101
Page generated: Mon Aug 12 05:35:02 2024
ISSN: ISSN 0027-8424
PubMed: 15333749
DOI: 10.1073/PNAS.0403045101
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