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Atomistry » Sodium » PDB 5cd1-5cwl » 5coq » |
Sodium in PDB 5coq: The Effect of Valine to Alanine Mutation on Inha Enzyme Crystallization Pattern and Substrate Binding Loop Conformation and FlexibilityEnzymatic activity of The Effect of Valine to Alanine Mutation on Inha Enzyme Crystallization Pattern and Substrate Binding Loop Conformation and Flexibility
All present enzymatic activity of The Effect of Valine to Alanine Mutation on Inha Enzyme Crystallization Pattern and Substrate Binding Loop Conformation and Flexibility:
1.3.1.9; Protein crystallography data
The structure of The Effect of Valine to Alanine Mutation on Inha Enzyme Crystallization Pattern and Substrate Binding Loop Conformation and Flexibility, PDB code: 5coq
was solved by
H.-J.Li,
C.-T.Lai,
N.Liu,
W.Yu,
S.Shah,
G.R.Bommineni,
V.Perrone,
M.Garcia-Diaz,
P.J.Tonge,
C.Simmerling,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Sodium Binding Sites:
The binding sites of Sodium atom in the The Effect of Valine to Alanine Mutation on Inha Enzyme Crystallization Pattern and Substrate Binding Loop Conformation and Flexibility
(pdb code 5coq). This binding sites where shown within
5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the The Effect of Valine to Alanine Mutation on Inha Enzyme Crystallization Pattern and Substrate Binding Loop Conformation and Flexibility, PDB code: 5coq: Sodium binding site 1 out of 1 in 5coqGo back to Sodium Binding Sites List in 5coq
Sodium binding site 1 out
of 1 in the The Effect of Valine to Alanine Mutation on Inha Enzyme Crystallization Pattern and Substrate Binding Loop Conformation and Flexibility
Mono view Stereo pair view
Reference:
C.T.Lai,
H.J.Li,
W.Yu,
S.Shah,
G.R.Bommineni,
V.Perrone,
M.Garcia-Diaz,
P.J.Tonge,
C.Simmerling.
Rational Modulation of the Induced-Fit Conformational Change For Slow-Onset Inhibition in Mycobacterium Tuberculosis Inha. Biochemistry V. 54 4683 2015.
Page generated: Tue Dec 15 10:46:44 2020
ISSN: ISSN 0006-2960 PubMed: 26147157 DOI: 10.1021/ACS.BIOCHEM.5B00284 |
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