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Atomistry » Potassium » PDB 1u1g-1w29 » 1usb | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Potassium » PDB 1u1g-1w29 » 1usb » |
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 A1-1Enzymatic 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; 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:
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:
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; Potassium binding site 1 out of 2 in 1usbGo back to![]() ![]()
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
Potassium binding site 2 out of 2 in 1usbGo back to![]() ![]()
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
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.
Page generated: Sat Aug 9 02:46:04 2025
ISSN: ISSN 0027-8424 PubMed: 15333749 DOI: 10.1073/PNAS.0403045101 |
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