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Magnesium in PDB 6rb7: Ruminococcus Gnavus Sialic Acid Aldolase Catalytic Lysine MutantProtein crystallography data
The structure of Ruminococcus Gnavus Sialic Acid Aldolase Catalytic Lysine Mutant, PDB code: 6rb7
was solved by
C.D.Owen,
A.Bell,
N.Juge,
M.A.Walsh,
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 Ruminococcus Gnavus Sialic Acid Aldolase Catalytic Lysine Mutant
(pdb code 6rb7). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the Ruminococcus Gnavus Sialic Acid Aldolase Catalytic Lysine Mutant, PDB code: 6rb7: Jump to Magnesium binding site number: 1; 2; 3; 4; Magnesium binding site 1 out of 4 in 6rb7Go back to Magnesium Binding Sites List in 6rb7
Magnesium binding site 1 out
of 4 in the Ruminococcus Gnavus Sialic Acid Aldolase Catalytic Lysine Mutant
Mono view Stereo pair view
Magnesium binding site 2 out of 4 in 6rb7Go back to Magnesium Binding Sites List in 6rb7
Magnesium binding site 2 out
of 4 in the Ruminococcus Gnavus Sialic Acid Aldolase Catalytic Lysine Mutant
Mono view Stereo pair view
Magnesium binding site 3 out of 4 in 6rb7Go back to Magnesium Binding Sites List in 6rb7
Magnesium binding site 3 out
of 4 in the Ruminococcus Gnavus Sialic Acid Aldolase Catalytic Lysine Mutant
Mono view Stereo pair view
Magnesium binding site 4 out of 4 in 6rb7Go back to Magnesium Binding Sites List in 6rb7
Magnesium binding site 4 out
of 4 in the Ruminococcus Gnavus Sialic Acid Aldolase Catalytic Lysine Mutant
Mono view Stereo pair view
Reference:
A.Bell,
J.Brunt,
E.Crost,
L.Vaux,
R.Nepravishta,
C.D.Owen,
D.Latousakis,
A.Xiao,
W.Li,
X.Chen,
M.A.Walsh,
J.Claesen,
J.Angulo,
G.H.Thomas,
N.Juge.
Elucidation of A Sialic Acid Metabolism Pathway in Mucus-Foraging Ruminococcus Gnavus Unravels Mechanisms of Bacterial Adaptation to the Gut. Nat Microbiol V. 4 2393 2019.
Page generated: Mon Dec 14 23:56:30 2020
ISSN: ESSN 2058-5276 PubMed: 31636419 DOI: 10.1038/S41564-019-0590-7 |
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