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Atomistry » Bromine » PDB 4z91-5c9w » 5c0u | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Bromine » PDB 4z91-5c9w » 5c0u » |
Bromine in PDB 5c0u: Crystal Structure of the Copper-Bound Form of Merb Mutant D99SEnzymatic activity of Crystal Structure of the Copper-Bound Form of Merb Mutant D99S
All present enzymatic activity of Crystal Structure of the Copper-Bound Form of Merb Mutant D99S:
4.99.1.2; Protein crystallography data
The structure of Crystal Structure of the Copper-Bound Form of Merb Mutant D99S, PDB code: 5c0u
was solved by
H.M.Wahba,
L.Lecoq,
M.Stevenson,
A.Mansour,
L.Cappadocia,
J.Lafrance-Vanasse,
K.J.Wilkinson,
J.Sygusch,
D.E.Wilcox,
J.G.Omichinski,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 5c0u:
The structure of Crystal Structure of the Copper-Bound Form of Merb Mutant D99S also contains other interesting chemical elements:
Bromine Binding Sites:
The binding sites of Bromine atom in the Crystal Structure of the Copper-Bound Form of Merb Mutant D99S
(pdb code 5c0u). This binding sites where shown within
5.0 Angstroms radius around Bromine atom.
In total only one binding site of Bromine was determined in the Crystal Structure of the Copper-Bound Form of Merb Mutant D99S, PDB code: 5c0u: Bromine binding site 1 out of 1 in 5c0uGo back to Bromine Binding Sites List in 5c0u
Bromine binding site 1 out
of 1 in the Crystal Structure of the Copper-Bound Form of Merb Mutant D99S
Mono view Stereo pair view
Reference:
H.M.Wahba,
L.Lecoq,
M.Stevenson,
A.Mansour,
L.Cappadocia,
J.Lafrance-Vanasse,
K.J.Wilkinson,
J.Sygusch,
D.E.Wilcox,
J.G.Omichinski.
Structural and Biochemical Characterization of A Copper-Binding Mutant of the Organomercurial Lyase Merb: Insight Into the Key Role of the Active Site Aspartic Acid in Hg-Carbon Bond Cleavage and Metal Binding Specificity. Biochemistry V. 55 1070 2016.
Page generated: Wed Jul 10 23:21:48 2024
ISSN: ISSN 0006-2960 PubMed: 26820485 DOI: 10.1021/ACS.BIOCHEM.5B01298 |
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