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Atomistry » Magnesium » PDB 1ueu-1v5f » 1ur2 » |
Magnesium in PDB 1ur2: Xylanase XYN10B Mutant (E262S) From Cellvibrio Mixtus in Complex with Arabinofuranose Alpha 1,3 Linked to XylotrioseEnzymatic activity of Xylanase XYN10B Mutant (E262S) From Cellvibrio Mixtus in Complex with Arabinofuranose Alpha 1,3 Linked to Xylotriose
All present enzymatic activity of Xylanase XYN10B Mutant (E262S) From Cellvibrio Mixtus in Complex with Arabinofuranose Alpha 1,3 Linked to Xylotriose:
3.2.1.8; Protein crystallography data
The structure of Xylanase XYN10B Mutant (E262S) From Cellvibrio Mixtus in Complex with Arabinofuranose Alpha 1,3 Linked to Xylotriose, PDB code: 1ur2
was solved by
G.Pell,
E.J.Taylor,
T.M.Gloster,
J.P.Turkenburg,
C.M.G.A.Fontes,
L.M.A.Ferreira,
G.J.Davies,
H.J.Gilbert,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 1ur2:
The structure of Xylanase XYN10B Mutant (E262S) From Cellvibrio Mixtus in Complex with Arabinofuranose Alpha 1,3 Linked to Xylotriose also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Xylanase XYN10B Mutant (E262S) From Cellvibrio Mixtus in Complex with Arabinofuranose Alpha 1,3 Linked to Xylotriose
(pdb code 1ur2). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Xylanase XYN10B Mutant (E262S) From Cellvibrio Mixtus in Complex with Arabinofuranose Alpha 1,3 Linked to Xylotriose, PDB code: 1ur2: Magnesium binding site 1 out of 1 in 1ur2Go back to Magnesium Binding Sites List in 1ur2
Magnesium binding site 1 out
of 1 in the Xylanase XYN10B Mutant (E262S) From Cellvibrio Mixtus in Complex with Arabinofuranose Alpha 1,3 Linked to Xylotriose
Mono view Stereo pair view
Reference:
G.Pell,
E.J.Taylor,
T.M.Gloster,
J.P.Turkenburg,
C.M.G.A.Fontes,
L.M.A.Ferreira,
T.Nagy,
S.Clark,
G.J.Davies,
H.J.Gilbert.
The Mechanisms By Which Family 10 Glycoside Hydrolases Bind Decorated Substrates J.Biol.Chem. V. 279 9597 2004.
Page generated: Mon Dec 14 06:53:31 2020
ISSN: ISSN 0021-9258 PubMed: 14668328 DOI: 10.1074/JBC.M312278200 |
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