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Potassium in PDB 6ab1: Crystal Structure of Methanosarcina Mazei Pylrs(Y306A/Y384F) Complexed with OazzlysEnzymatic activity of Crystal Structure of Methanosarcina Mazei Pylrs(Y306A/Y384F) Complexed with Oazzlys
All present enzymatic activity of Crystal Structure of Methanosarcina Mazei Pylrs(Y306A/Y384F) Complexed with Oazzlys:
6.1.1.26; Protein crystallography data
The structure of Crystal Structure of Methanosarcina Mazei Pylrs(Y306A/Y384F) Complexed with Oazzlys, PDB code: 6ab1
was solved by
T.Yanagisawa,
M.Kuratani,
S.Yokoyama,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 6ab1:
The structure of Crystal Structure of Methanosarcina Mazei Pylrs(Y306A/Y384F) Complexed with Oazzlys also contains other interesting chemical elements:
Potassium Binding Sites:
The binding sites of Potassium atom in the Crystal Structure of Methanosarcina Mazei Pylrs(Y306A/Y384F) Complexed with Oazzlys
(pdb code 6ab1). This binding sites where shown within
5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Crystal Structure of Methanosarcina Mazei Pylrs(Y306A/Y384F) Complexed with Oazzlys, PDB code: 6ab1: Jump to Potassium binding site number: 1; 2; Potassium binding site 1 out of 2 in 6ab1Go back to Potassium Binding Sites List in 6ab1
Potassium binding site 1 out
of 2 in the Crystal Structure of Methanosarcina Mazei Pylrs(Y306A/Y384F) Complexed with Oazzlys
Mono view Stereo pair view
Potassium binding site 2 out of 2 in 6ab1Go back to Potassium Binding Sites List in 6ab1
Potassium binding site 2 out
of 2 in the Crystal Structure of Methanosarcina Mazei Pylrs(Y306A/Y384F) Complexed with Oazzlys
Mono view Stereo pair view
Reference:
T.Yanagisawa,
M.Kuratani,
E.Seki,
N.Hino,
K.Sakamoto,
S.Yokoyama.
Structural Basis For Genetic-Code Expansion with Bulky Lysine Derivatives By An Engineered Pyrrolysyl-Trna Synthetase. Cell Chem Biol V. 26 936 2019.
Page generated: Mon Dec 14 00:16:59 2020
ISSN: ESSN 2451-9456 PubMed: 31031143 DOI: 10.1016/J.CHEMBIOL.2019.03.008 |
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