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Atomistry » Magnesium » PDB 6ly6-6m65 » 6lya | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Magnesium » PDB 6ly6-6m65 » 6lya » |
Magnesium in PDB 6lya: Pylrs C-Terminus Domain Mutant Bound with 1-Methyl-L-Tryptophan and AmpnpEnzymatic activity of Pylrs C-Terminus Domain Mutant Bound with 1-Methyl-L-Tryptophan and Ampnp
All present enzymatic activity of Pylrs C-Terminus Domain Mutant Bound with 1-Methyl-L-Tryptophan and Ampnp:
6.1.1.26; Protein crystallography data
The structure of Pylrs C-Terminus Domain Mutant Bound with 1-Methyl-L-Tryptophan and Ampnp, PDB code: 6lya
was solved by
J.H.Weng,
M.D.Tsai,
Y.S.Wang,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Pylrs C-Terminus Domain Mutant Bound with 1-Methyl-L-Tryptophan and Ampnp
(pdb code 6lya). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Pylrs C-Terminus Domain Mutant Bound with 1-Methyl-L-Tryptophan and Ampnp, PDB code: 6lya: Jump to Magnesium binding site number: 1; 2; Magnesium binding site 1 out of 2 in 6lyaGo back to![]() ![]()
Magnesium binding site 1 out
of 2 in the Pylrs C-Terminus Domain Mutant Bound with 1-Methyl-L-Tryptophan and Ampnp
![]() Mono view ![]() Stereo pair view
Magnesium binding site 2 out of 2 in 6lyaGo back to![]() ![]()
Magnesium binding site 2 out
of 2 in the Pylrs C-Terminus Domain Mutant Bound with 1-Methyl-L-Tryptophan and Ampnp
![]() Mono view ![]() Stereo pair view
Reference:
H.K.Jiang,
Y.H.Wang,
J.H.Weng,
P.Kurkute,
C.L.Li,
M.N.Lee,
P.J.Chen,
H.W.Tseng,
M.D.Tsai,
Y.S.Wang.
Probing the Active Site of Deubiquitinase USP30 with Noncanonical Tryptophan Analogues. Biochemistry V. 59 2205 2020.
Page generated: Tue Oct 1 10:47:54 2024
ISSN: ISSN 0006-2960 PubMed: 32484330 DOI: 10.1021/ACS.BIOCHEM.0C00307 |
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