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Magnesium in PDB 2c71: The Structure of A Family 4 Acetyl Xylan Esterase From Clostridium Thermocellum in Complex with A Magnesium Ion.

Enzymatic activity of The Structure of A Family 4 Acetyl Xylan Esterase From Clostridium Thermocellum in Complex with A Magnesium Ion.

All present enzymatic activity of The Structure of A Family 4 Acetyl Xylan Esterase From Clostridium Thermocellum in Complex with A Magnesium Ion.:
3.1.1.72;

Protein crystallography data

The structure of The Structure of A Family 4 Acetyl Xylan Esterase From Clostridium Thermocellum in Complex with A Magnesium Ion., PDB code: 2c71 was solved by E.J.Taylor, P.J.Turkenburg, F.Vincent, A.M.Brzozowski, T.M.Gloster, C.Dupont, F.Shareck, M.S.J.Centeno, J.A.M.Prates, L.M.A.Ferreira, C.M.G.A.Fontes, P.Biely, G.J.Davies, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 28.41 / 1.05
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 106.064, 106.064, 35.466, 90.00, 90.00, 90.00
R / Rfree (%) 12.4 / 14.2

Magnesium Binding Sites:

The binding sites of Magnesium atom in the The Structure of A Family 4 Acetyl Xylan Esterase From Clostridium Thermocellum in Complex with A Magnesium Ion. (pdb code 2c71). 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 The Structure of A Family 4 Acetyl Xylan Esterase From Clostridium Thermocellum in Complex with A Magnesium Ion., PDB code: 2c71:

Magnesium binding site 1 out of 1 in 2c71

Go back to Magnesium Binding Sites List in 2c71
Magnesium binding site 1 out of 1 in the The Structure of A Family 4 Acetyl Xylan Esterase From Clostridium Thermocellum in Complex with A Magnesium Ion.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of The Structure of A Family 4 Acetyl Xylan Esterase From Clostridium Thermocellum in Complex with A Magnesium Ion. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1692

b:5.8
occ:1.00
 O A:HOH2230 2.0 7.2 1.0
O A:HOH2100 2.0 7.8 1.0
O A:HOH2026 2.1 8.3 1.0
OD1 A:ASP488 2.1 6.2 1.0
O A:HOH2163 2.2 8.2 1.0
NE2 A:HIS539 2.2 5.4 1.0
CG A:ASP488 3.1 6.2 1.0
CE1 A:HIS539 3.2 5.6 1.0
CD2 A:HIS539 3.2 5.1 1.0
OD2 A:ASP488 3.4 8.5 1.0
O A:HOH2102 4.1 7.3 1.0
O A:HOH2025 4.1 11.3 1.0
O A:HOH2161 4.1 16.9 1.0
CB A:ASP487 4.2 5.9 1.0
O A:HOH2103 4.2 16.0 1.0
OD2 A:ASP487 4.3 8.4 1.0
ND1 A:HIS539 4.3 5.8 1.0
CG A:HIS539 4.4 4.9 1.0
O A:HOH2229 4.4 20.0 1.0
NE2 A:HIS630 4.4 9.4 1.0
CB A:ASP488 4.5 5.4 1.0
CD2 A:HIS630 4.6 7.8 1.0
CG A:ASP487 4.6 7.5 1.0
CD1 A:TYR543 4.9 7.8 1.0
CA A:ASP488 4.9 4.8 1.0
N A:ASP488 5.0 5.0 1.0

Reference:

E.J.Taylor, T.M.Gloster, P.J.Turkenburg, F.Vincent, A.M.Brzozowski, C.Dupont, F.Shareck, M.S.J.Centeno, J.A.M.Prates, L.M.A.Ferreira, C.M.G.A.Fontes, P.Biely, G.J.Davies. Structure and Activity of Two Metal-Ion Dependent Acetyl Xylan Esterases Involved in Plant Cell-Wall Degradation Reveals A Close Similarity to Peptidoglycan Deacetylases. J.Biol.Chem. V. 281 10968 2006.
ISSN: ISSN 0021-9258
PubMed: 16431911
DOI: 10.1074/JBC.M513066200
Page generated: Tue Aug 13 22:12:50 2024

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