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Atomistry » Magnesium » PDB 2r20-2reu » 2rav | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Magnesium » PDB 2r20-2reu » 2rav » |
Magnesium in PDB 2rav: X-Ray Crystallographic Structures Show Conservation of A Trigonal- Bipyramidal Intermediate in A Phosphoryl-Transfer Superfamily.Protein crystallography data
The structure of X-Ray Crystallographic Structures Show Conservation of A Trigonal- Bipyramidal Intermediate in A Phosphoryl-Transfer Superfamily., PDB code: 2rav
was solved by
Z.Lu,
D.Dunaway-Mariano,
K.N.Allen,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 2rav:
The structure of X-Ray Crystallographic Structures Show Conservation of A Trigonal- Bipyramidal Intermediate in A Phosphoryl-Transfer Superfamily. also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the X-Ray Crystallographic Structures Show Conservation of A Trigonal- Bipyramidal Intermediate in A Phosphoryl-Transfer Superfamily.
(pdb code 2rav). 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 X-Ray Crystallographic Structures Show Conservation of A Trigonal- Bipyramidal Intermediate in A Phosphoryl-Transfer Superfamily., PDB code: 2rav: Magnesium binding site 1 out of 1 in 2ravGo back to Magnesium Binding Sites List in 2rav
Magnesium binding site 1 out
of 1 in the X-Ray Crystallographic Structures Show Conservation of A Trigonal- Bipyramidal Intermediate in A Phosphoryl-Transfer Superfamily.
Mono view Stereo pair view
Reference:
Z.Lu,
D.Dunaway-Mariano,
K.N.Allen.
The Catalytic Scaffold of the Haloalkanoic Acid Dehalogenase Enzyme Superfamily Acts As A Mold For the Trigonal Bipyramidal Transition State. Proc.Natl.Acad.Sci.Usa V. 105 5687 2008.
Page generated: Wed Aug 14 03:19:50 2024
ISSN: ISSN 0027-8424 PubMed: 18398008 DOI: 10.1073/PNAS.0710800105 |
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