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Atomistry » Magnesium » PDB 2q9y-2qrf » 2qin | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Magnesium » PDB 2q9y-2qrf » 2qin » |
Magnesium in PDB 2qin: Stenotrophomonas Maltophilia L1 Metallo-Beta-Lactamase Asp-120 Cys MutantEnzymatic activity of Stenotrophomonas Maltophilia L1 Metallo-Beta-Lactamase Asp-120 Cys Mutant
All present enzymatic activity of Stenotrophomonas Maltophilia L1 Metallo-Beta-Lactamase Asp-120 Cys Mutant:
3.5.2.6; Protein crystallography data
The structure of Stenotrophomonas Maltophilia L1 Metallo-Beta-Lactamase Asp-120 Cys Mutant, PDB code: 2qin
was solved by
J.Spencer,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 2qin:
The structure of Stenotrophomonas Maltophilia L1 Metallo-Beta-Lactamase Asp-120 Cys Mutant also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Stenotrophomonas Maltophilia L1 Metallo-Beta-Lactamase Asp-120 Cys Mutant
(pdb code 2qin). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Stenotrophomonas Maltophilia L1 Metallo-Beta-Lactamase Asp-120 Cys Mutant, PDB code: 2qin: Jump to Magnesium binding site number: 1; 2; Magnesium binding site 1 out of 2 in 2qinGo back to Magnesium Binding Sites List in 2qin
Magnesium binding site 1 out
of 2 in the Stenotrophomonas Maltophilia L1 Metallo-Beta-Lactamase Asp-120 Cys Mutant
Mono view Stereo pair view
Magnesium binding site 2 out of 2 in 2qinGo back to Magnesium Binding Sites List in 2qin
Magnesium binding site 2 out
of 2 in the Stenotrophomonas Maltophilia L1 Metallo-Beta-Lactamase Asp-120 Cys Mutant
Mono view Stereo pair view
Reference:
J.Crisp,
R.Conners,
J.D.Garrity,
A.L.Carenbauer,
M.W.Crowder,
J.Spencer.
Structural Basis For the Role of Asp-120 in Metallo-Beta-Lactamases. Biochemistry V. 46 10664 2007.
Page generated: Wed Aug 14 02:44:32 2024
ISSN: ISSN 0006-2960 PubMed: 17715946 DOI: 10.1021/BI700707U |
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