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Magnesium in PDB 1bpm: Differentiation and Identification of the Two Catalytic Metal Binding Sites in Bovine Lens Leucine Aminopeptidase By X-Ray CrystallographyEnzymatic activity of Differentiation and Identification of the Two Catalytic Metal Binding Sites in Bovine Lens Leucine Aminopeptidase By X-Ray Crystallography
All present enzymatic activity of Differentiation and Identification of the Two Catalytic Metal Binding Sites in Bovine Lens Leucine Aminopeptidase By X-Ray Crystallography:
3.4.11.1; Protein crystallography data
The structure of Differentiation and Identification of the Two Catalytic Metal Binding Sites in Bovine Lens Leucine Aminopeptidase By X-Ray Crystallography, PDB code: 1bpm
was solved by
H.Kim,
W.N.Lipscomb,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 1bpm:
The structure of Differentiation and Identification of the Two Catalytic Metal Binding Sites in Bovine Lens Leucine Aminopeptidase By X-Ray Crystallography also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Differentiation and Identification of the Two Catalytic Metal Binding Sites in Bovine Lens Leucine Aminopeptidase By X-Ray Crystallography
(pdb code 1bpm). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Differentiation and Identification of the Two Catalytic Metal Binding Sites in Bovine Lens Leucine Aminopeptidase By X-Ray Crystallography, PDB code: 1bpm: Magnesium binding site 1 out of 1 in 1bpmGo back to![]() ![]()
Magnesium binding site 1 out
of 1 in the Differentiation and Identification of the Two Catalytic Metal Binding Sites in Bovine Lens Leucine Aminopeptidase By X-Ray Crystallography
![]() Mono view ![]() Stereo pair view
Reference:
H.Kim,
W.N.Lipscomb.
Differentiation and Identification of the Two Catalytic Metal Binding Sites in Bovine Lens Leucine Aminopeptidase By X-Ray Crystallography. Proc.Natl.Acad.Sci.Usa V. 90 5006 1993.
Page generated: Mon Dec 14 05:48:05 2020
ISSN: ISSN 0027-8424 PubMed: 8506345 DOI: 10.1073/PNAS.90.11.5006 |
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