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Atomistry » Calcium » PDB 7l74-7lrx » 7lj2 » |
Calcium in PDB 7lj2: Structure of Exo-L-Galactose-6-Sulfatase BUS1_11 From Bacteroides Uniformis in Complex with NeoporphyrabioseProtein crystallography data
The structure of Structure of Exo-L-Galactose-6-Sulfatase BUS1_11 From Bacteroides Uniformis in Complex with Neoporphyrabiose, PDB code: 7lj2
was solved by
C.S.Robb,
A.B.Boraston,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 7lj2:
The structure of Structure of Exo-L-Galactose-6-Sulfatase BUS1_11 From Bacteroides Uniformis in Complex with Neoporphyrabiose also contains other interesting chemical elements:
Calcium Binding Sites:
The binding sites of Calcium atom in the Structure of Exo-L-Galactose-6-Sulfatase BUS1_11 From Bacteroides Uniformis in Complex with Neoporphyrabiose
(pdb code 7lj2). This binding sites where shown within
5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Structure of Exo-L-Galactose-6-Sulfatase BUS1_11 From Bacteroides Uniformis in Complex with Neoporphyrabiose, PDB code: 7lj2: Jump to Calcium binding site number: 1; 2; Calcium binding site 1 out of 2 in 7lj2Go back to![]() ![]()
Calcium binding site 1 out
of 2 in the Structure of Exo-L-Galactose-6-Sulfatase BUS1_11 From Bacteroides Uniformis in Complex with Neoporphyrabiose
![]() Mono view ![]() Stereo pair view
Calcium binding site 2 out of 2 in 7lj2Go back to![]() ![]()
Calcium binding site 2 out
of 2 in the Structure of Exo-L-Galactose-6-Sulfatase BUS1_11 From Bacteroides Uniformis in Complex with Neoporphyrabiose
![]() Mono view ![]() Stereo pair view
Reference:
C.S.Robb,
J.K.Hobbs,
B.Pluvinage,
G.Reintjes,
L.Klassen,
S.Monteith,
G.Giljan,
C.Amundsen,
C.Vickers,
A.G.Hettle,
R.Hills,
X.Xing,
T.Montina,
W.F.Zandberg,
D.W.Abbott,
A.B.Boraston.
Metabolism of A Hybrid Algal Galactan By Members of the Human Gut Microbiome. Nat.Chem.Biol. V. 18 501 2022.
Page generated: Wed Jul 9 23:11:35 2025
ISSN: ESSN 1552-4469 PubMed: 35289327 DOI: 10.1038/S41589-022-00983-Y |
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