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Atomistry » Calcium » PDB 2xqg-2y6h » 2xsg | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Calcium » PDB 2xqg-2y6h » 2xsg » |
Calcium in PDB 2xsg: Structure of the GH92 Family Glycosyl Hydrolase CCMAN5Enzymatic activity of Structure of the GH92 Family Glycosyl Hydrolase CCMAN5
All present enzymatic activity of Structure of the GH92 Family Glycosyl Hydrolase CCMAN5:
3.2.1.24; Protein crystallography data
The structure of Structure of the GH92 Family Glycosyl Hydrolase CCMAN5, PDB code: 2xsg
was solved by
E.Baranova,
P.Tiels,
H.Remaut,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Calcium Binding Sites:
The binding sites of Calcium atom in the Structure of the GH92 Family Glycosyl Hydrolase CCMAN5
(pdb code 2xsg). 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 the GH92 Family Glycosyl Hydrolase CCMAN5, PDB code: 2xsg: Jump to Calcium binding site number: 1; 2; Calcium binding site 1 out of 2 in 2xsgGo back to Calcium Binding Sites List in 2xsg
Calcium binding site 1 out
of 2 in the Structure of the GH92 Family Glycosyl Hydrolase CCMAN5
Mono view Stereo pair view
Calcium binding site 2 out of 2 in 2xsgGo back to Calcium Binding Sites List in 2xsg
Calcium binding site 2 out
of 2 in the Structure of the GH92 Family Glycosyl Hydrolase CCMAN5
Mono view Stereo pair view
Reference:
P.Tiels,
E.Baranova,
K.Piens,
C.De Visscher,
G.Pynaert,
W.Nerinckx,
J.Stout,
F.Fudalej,
P.Hulpiau,
S.Tannler,
S.Geysens,
A.Van Hecke,
A.Valevska,
W.Vervecken,
H.Remaut,
N.Callewaert.
A Bacterial Glycosidase Enables Mannose-6-Phosphate Modification and Improved Cellular Uptake of Yeast-Produced Recombinant Human Lysosomal Enzymes. Nat.Biotechnol. V. 30 1225 2012.
Page generated: Sat Dec 12 03:59:23 2020
ISSN: ISSN 1087-0156 PubMed: 23159880 DOI: 10.1038/NBT.2427 |
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