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Atomistry » Potassium » PDB 7c1o-7fs0 » 7fha | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Potassium » PDB 7c1o-7fs0 » 7fha » |
Potassium in PDB 7fha: Crystal Structure of the Atp Sulfurylase Domain of Human PAPSS2 in Complex with ApsEnzymatic activity of Crystal Structure of the Atp Sulfurylase Domain of Human PAPSS2 in Complex with Aps
All present enzymatic activity of Crystal Structure of the Atp Sulfurylase Domain of Human PAPSS2 in Complex with Aps:
2.7.1.25; 2.7.7.4; Protein crystallography data
The structure of Crystal Structure of the Atp Sulfurylase Domain of Human PAPSS2 in Complex with Aps, PDB code: 7fha
was solved by
P.Zhang,
L.Zhang,
L.Zhang,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Potassium Binding Sites:
The binding sites of Potassium atom in the Crystal Structure of the Atp Sulfurylase Domain of Human PAPSS2 in Complex with Aps
(pdb code 7fha). This binding sites where shown within
5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Crystal Structure of the Atp Sulfurylase Domain of Human PAPSS2 in Complex with Aps, PDB code: 7fha: Jump to Potassium binding site number: 1; 2; Potassium binding site 1 out of 2 in 7fhaGo back to![]() ![]()
Potassium binding site 1 out
of 2 in the Crystal Structure of the Atp Sulfurylase Domain of Human PAPSS2 in Complex with Aps
![]() Mono view ![]() Stereo pair view
Potassium binding site 2 out of 2 in 7fhaGo back to![]() ![]()
Potassium binding site 2 out
of 2 in the Crystal Structure of the Atp Sulfurylase Domain of Human PAPSS2 in Complex with Aps
![]() Mono view ![]() Stereo pair view
Reference:
P.Zhang,
L.Zhang,
Z.Hou,
H.Liu,
H.Gao,
L.Zhang.
Structural Basis For the Substrate Recognition Mechanism of Atp-Sulfurylase Domain of Human Paps Synthase 2 Biochem.Biophys.Res.Commun. V. 586 2022.
Page generated: Mon Aug 12 18:55:34 2024
ISSN: ESSN 1090-2104 DOI: 10.1016/J.BBRC.2021.11.062 |
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