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Atomistry » Calcium » PDB 5a3y-5afb » 5a9s | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Calcium » PDB 5a3y-5afb » 5a9s » |
Calcium in PDB 5a9s: Nadph Complex of Imine Reductase From Amycolatopsis OrientalisEnzymatic activity of Nadph Complex of Imine Reductase From Amycolatopsis Orientalis
All present enzymatic activity of Nadph Complex of Imine Reductase From Amycolatopsis Orientalis:
1.5.1.48; Protein crystallography data
The structure of Nadph Complex of Imine Reductase From Amycolatopsis Orientalis, PDB code: 5a9s
was solved by
H.Man,
G.Aleku,
N.J.Turner,
G.Grogan,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Calcium Binding Sites:
The binding sites of Calcium atom in the Nadph Complex of Imine Reductase From Amycolatopsis Orientalis
(pdb code 5a9s). This binding sites where shown within
5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Nadph Complex of Imine Reductase From Amycolatopsis Orientalis, PDB code: 5a9s: Jump to Calcium binding site number: 1; 2; Calcium binding site 1 out of 2 in 5a9sGo back to Calcium Binding Sites List in 5a9s
Calcium binding site 1 out
of 2 in the Nadph Complex of Imine Reductase From Amycolatopsis Orientalis
Mono view Stereo pair view
Calcium binding site 2 out of 2 in 5a9sGo back to Calcium Binding Sites List in 5a9s
Calcium binding site 2 out
of 2 in the Nadph Complex of Imine Reductase From Amycolatopsis Orientalis
Mono view Stereo pair view
Reference:
G.A.Aleku,
H.Man,
S.P.France,
F.Leipold,
S.Hussain,
L.Toca-Gonzalez,
R.Marchington,
S.Hart,
J.P.Turkenburg,
G.Grogan,
N.J.Turner.
Stereoselectivity and Structural Characterization of An Imine Reductase (Ired) From Amycolatopsis Orientalis Acs Catalysis V. 6 3880 2016.
Page generated: Sat Dec 12 05:17:00 2020
ISSN: ESSN 2155-5435 DOI: 10.1021/ACSCATAL.6B00782 |
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