|
Atomistry » Magnesium » PDB 1k9w-1kk3 » 1khk | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Magnesium » PDB 1k9w-1kk3 » 1khk » |
Magnesium in PDB 1khk: E. Coli Alkaline Phosphatase Mutant (D153HD330N)Enzymatic activity of E. Coli Alkaline Phosphatase Mutant (D153HD330N)
All present enzymatic activity of E. Coli Alkaline Phosphatase Mutant (D153HD330N):
3.1.3.1; Protein crystallography data
The structure of E. Coli Alkaline Phosphatase Mutant (D153HD330N), PDB code: 1khk
was solved by
M.H.Le Du,
C.Lamoure,
B.H.Muller,
O.V.Bulgakov,
E.Lajeunesse,
A.Menez,
J.C.Boulain,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 1khk:
The structure of E. Coli Alkaline Phosphatase Mutant (D153HD330N) also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the E. Coli Alkaline Phosphatase Mutant (D153HD330N)
(pdb code 1khk). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the E. Coli Alkaline Phosphatase Mutant (D153HD330N), PDB code: 1khk: Jump to Magnesium binding site number: 1; 2; Magnesium binding site 1 out of 2 in 1khkGo back to Magnesium Binding Sites List in 1khk
Magnesium binding site 1 out
of 2 in the E. Coli Alkaline Phosphatase Mutant (D153HD330N)
Mono view Stereo pair view
Magnesium binding site 2 out of 2 in 1khkGo back to Magnesium Binding Sites List in 1khk
Magnesium binding site 2 out
of 2 in the E. Coli Alkaline Phosphatase Mutant (D153HD330N)
Mono view Stereo pair view
Reference:
M.H.Le Du,
C.Lamoure,
B.H.Muller,
O.V.Bulgakov,
E.Lajeunesse,
A.Menez,
J.C.Boulain.
Artificial Evolution of An Enzyme Active Site: Structural Studies of Three Highly Active Mutants of Escherichia Coli Alkaline Phosphatase. J.Mol.Biol. V. 316 941 2002.
Page generated: Mon Dec 14 06:20:24 2020
ISSN: ISSN 0022-2836 PubMed: 11884134 DOI: 10.1006/JMBI.2001.5384 |
Last articlesZn in 8WB0Zn in 8WAX Zn in 8WAU Zn in 8WAZ Zn in 8WAY Zn in 8WAV Zn in 8WAW Zn in 8WAT Zn in 8W7M Zn in 8WD3 |
© Copyright 2008-2020 by atomistry.com | ||
Home | Site Map | Copyright | Contact us | Privacy |