Magnesium in PDB 1uqy: Xylanase XYN10B Mutant (E262S) From Cellvibrio Mixtus in Complex with Xylopentaose

All present enzymatic activity of Xylanase XYN10B Mutant (E262S) From Cellvibrio Mixtus in Complex with Xylopentaose:
3.2.1.8;

The structure of Xylanase XYN10B Mutant (E262S) From Cellvibrio Mixtus in Complex with Xylopentaose, PDB code: 1uqy 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:

Resolution Low / High (Å)	56.80 / 1.72
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	47.158, 67.901, 104.794, 90.00, 90.00, 90.00
R / Rfree (%)	14 / 18.6

The binding sites of Magnesium atom in the Xylanase XYN10B Mutant (E262S) From Cellvibrio Mixtus in Complex with Xylopentaose (pdb code 1uqy). 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 Xylopentaose, PDB code: 1uqy:

Magnesium binding site 1 out of 1 in the Xylanase XYN10B Mutant (E262S) From Cellvibrio Mixtus in Complex with Xylopentaose


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Xylanase XYN10B Mutant (E262S) From Cellvibrio Mixtus in Complex with Xylopentaose within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1380 b:19.3 occ:1.00 O A:HOH2081 2.0 20.7 1.0 O A:HOH2308 2.1 18.8 1.0 O A:HOH2076 2.1 19.9 1.0 O A:HOH2310 2.1 16.4 1.0 O A:HOH2075 2.1 20.5 1.0 O A:HOH2167 2.3 15.6 1.0 O A:HOH2182 4.0 26.2 1.0 O A:HOH2127 4.2 39.7 1.0 O A:HOH2168 4.3 16.5 1.0 O A:GLY147 4.3 13.5 1.0 O A:HOH2179 4.4 22.0 1.0 O A:LYS148 4.4 10.7 1.0 CA A:LYS148 4.4 11.7 1.0 OG1 A:THR95 4.6 10.3 1.0 O A:HOH2307 4.9 38.6 1.0 O A:HOH2126 4.9 40.4 1.0 C A:LYS148 4.9 10.9 1.0 CG2 A:THR95 4.9 9.8 1.0

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.
ISSN: ISSN 0021-9258
PubMed: 14668328
DOI: 10.1074/JBC.M312278200