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Magnesium in PDB 1uqz: Xylanase XYN10B Mutant (E262S) From Cellvibrio Mixtus in Complex with 4-O-Methyl Glucuronic Acid

Enzymatic activity of Xylanase XYN10B Mutant (E262S) From Cellvibrio Mixtus in Complex with 4-O-Methyl Glucuronic Acid

All present enzymatic activity of Xylanase XYN10B Mutant (E262S) From Cellvibrio Mixtus in Complex with 4-O-Methyl Glucuronic Acid:
3.2.1.8;

Protein crystallography data

The structure of Xylanase XYN10B Mutant (E262S) From Cellvibrio Mixtus in Complex with 4-O-Methyl Glucuronic Acid, PDB code: 1uqz 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) 14.82 / 1.55
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 47.148, 68.117, 105.086, 90.00, 90.00, 90.00
R / Rfree (%) 15.8 / 19.9

Other elements in 1uqz:

The structure of Xylanase XYN10B Mutant (E262S) From Cellvibrio Mixtus in Complex with 4-O-Methyl Glucuronic Acid also contains other interesting chemical elements:

Chlorine (Cl) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Xylanase XYN10B Mutant (E262S) From Cellvibrio Mixtus in Complex with 4-O-Methyl Glucuronic Acid (pdb code 1uqz). 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 4-O-Methyl Glucuronic Acid, PDB code: 1uqz:

Magnesium binding site 1 out of 1 in 1uqz

Go back to Magnesium Binding Sites List in 1uqz
Magnesium binding site 1 out of 1 in the Xylanase XYN10B Mutant (E262S) From Cellvibrio Mixtus in Complex with 4-O-Methyl Glucuronic Acid


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 4-O-Methyl Glucuronic Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1382

b:9.5
occ:1.00
 O A:HOH2087 2.0 13.3 1.0
O A:HOH2328 2.0 12.6 1.0
O A:HOH2331 2.1 11.8 1.0
O A:HOH2083 2.1 11.6 1.0
O A:HOH2082 2.1 13.0 1.0
O A:HOH2179 2.2 10.7 1.0
O A:HOH2196 4.0 16.7 1.0
O A:HOH2141 4.2 41.8 1.0
O A:HOH2181 4.2 10.6 1.0
O A:HOH2139 4.3 25.4 1.0
O A:HOH2191 4.4 13.2 1.0
O A:GLY147 4.4 8.8 1.0
O A:LYS148 4.4 7.4 1.0
CA A:LYS148 4.5 6.3 1.0
OG1 A:THR95 4.5 5.2 1.0
O A:HOH2089 4.7 33.3 1.0
CG2 A:THR95 4.8 7.8 1.0
C A:LYS148 5.0 6.4 1.0

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.
ISSN: ISSN 0021-9258
PubMed: 14668328
DOI: 10.1074/JBC.M312278200
Page generated: Tue Aug 13 14:54:41 2024

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