Magnesium in PDB 2fgl: An Alkali Thermostable F/10 Xylanase From Alkalophilic Bacillus Sp. Ng-27

All present enzymatic activity of An Alkali Thermostable F/10 Xylanase From Alkalophilic Bacillus Sp. Ng-27:
3.2.1.8;

The structure of An Alkali Thermostable F/10 Xylanase From Alkalophilic Bacillus Sp. Ng-27, PDB code: 2fgl was solved by S.Ramakumar, K.Manikandan, A.Bhardwaj, V.S.Reddy, N.K.Lokanath, A.Ghosh, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	49.00 / 2.20
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	59.188, 84.200, 174.701, 90.00, 90.00, 90.00
R / Rfree (%)	21.8 / 25.8

The binding sites of Magnesium atom in the An Alkali Thermostable F/10 Xylanase From Alkalophilic Bacillus Sp. Ng-27 (pdb code 2fgl). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the An Alkali Thermostable F/10 Xylanase From Alkalophilic Bacillus Sp. Ng-27, PDB code: 2fgl:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in the An Alkali Thermostable F/10 Xylanase From Alkalophilic Bacillus Sp. Ng-27


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of An Alkali Thermostable F/10 Xylanase From Alkalophilic Bacillus Sp. Ng-27 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg601 b:37.2 occ:1.00 O A:ARG351 2.0 47.0 1.0 OD1 A:ASN292 2.1 44.0 1.0 OD2 A:ASP354 2.7 63.1 1.0 C A:ARG351 3.2 45.6 1.0 CG A:ASN292 3.3 44.1 1.0 CG A:ASP354 3.8 59.5 1.0 CA A:ILE352 4.1 41.0 1.0 N A:ILE352 4.1 44.4 1.0 CB A:ASN292 4.2 42.5 1.0 CA A:ARG351 4.2 45.5 1.0 OD1 A:ASP354 4.2 62.6 1.0 ND2 A:ASN292 4.2 45.4 1.0 O A:HOH764 4.3 36.1 1.0 CA A:ASN292 4.3 41.0 1.0 O A:ASP354 4.4 53.8 1.0 OE2 A:GLU296 4.5 57.0 1.0 O A:ASN292 4.6 38.8 1.0 C A:ASP354 4.7 52.6 1.0 CB A:ARG351 4.7 45.3 1.0 C A:ILE352 4.8 40.6 1.0 C A:ASN292 4.9 41.6 1.0

Magnesium binding site 2 out of 4 in the An Alkali Thermostable F/10 Xylanase From Alkalophilic Bacillus Sp. Ng-27


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of An Alkali Thermostable F/10 Xylanase From Alkalophilic Bacillus Sp. Ng-27 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg602 b:46.8 occ:1.00 O A:SER18 2.4 45.5 1.0 O A:ASP302 2.5 49.5 1.0 O A:LEU305 2.5 36.2 1.0 O A:HOH884 2.8 46.9 1.0 O A:HOH907 3.3 62.3 1.0 C A:LEU305 3.5 39.5 1.0 C A:SER18 3.6 45.3 1.0 C A:ASP302 3.6 49.2 1.0 CA A:SER306 3.9 39.0 1.0 N A:SER306 4.1 38.4 1.0 CA A:ASP302 4.3 49.7 1.0 CA A:SER18 4.5 47.1 1.0 N A:LEU305 4.5 44.6 1.0 CB A:ASP302 4.5 51.6 1.0 N A:PHE19 4.5 44.3 1.0 CB A:PHE19 4.5 40.5 1.0 CA A:PHE19 4.6 42.4 1.0 CB A:SER306 4.6 38.1 1.0 CA A:LEU305 4.7 41.5 1.0 O A:HOH769 4.7 42.3 1.0 N A:ALA303 4.7 48.9 1.0 C A:SER306 4.8 38.0 1.0 CA A:ALA303 4.8 49.0 1.0 C A:ALA303 4.9 47.7 1.0 O A:SER306 4.9 39.7 1.0

Magnesium binding site 3 out of 4 in the An Alkali Thermostable F/10 Xylanase From Alkalophilic Bacillus Sp. Ng-27


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of An Alkali Thermostable F/10 Xylanase From Alkalophilic Bacillus Sp. Ng-27 within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg603 b:47.7 occ:1.00 O B:ARG351 2.0 48.0 1.0 OD1 B:ASN292 2.1 48.0 1.0 O B:HOH845 2.6 49.8 1.0 OD2 B:ASP354 2.6 61.5 1.0 C B:ARG351 3.2 45.8 1.0 CG B:ASN292 3.3 47.5 1.0 CG B:ASP354 3.7 59.4 1.0 CA B:ILE352 4.1 42.1 1.0 N B:ILE352 4.1 44.2 1.0 OD1 B:ASP354 4.1 62.2 1.0 CA B:ARG351 4.2 45.5 1.0 CB B:ASN292 4.2 46.1 1.0 ND2 B:ASN292 4.3 47.2 1.0 CA B:ASN292 4.4 44.1 1.0 O B:ASP354 4.4 54.2 1.0 OE2 B:GLU296 4.5 57.8 1.0 O B:ASN292 4.6 46.5 1.0 O B:HOH772 4.6 56.8 1.0 C B:ASP354 4.7 52.8 1.0 C B:ILE352 4.7 41.9 1.0 CB B:ARG351 4.8 45.5 1.0 C B:ASN292 4.9 44.4 1.0

Magnesium binding site 4 out of 4 in the An Alkali Thermostable F/10 Xylanase From Alkalophilic Bacillus Sp. Ng-27


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of An Alkali Thermostable F/10 Xylanase From Alkalophilic Bacillus Sp. Ng-27 within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg604 b:39.5 occ:0.50 O B:ASP302 2.1 53.1 1.0 O B:SER18 2.4 48.6 1.0 O B:LEU305 2.5 41.8 1.0 C B:ASP302 3.3 53.2 1.0 C B:LEU305 3.5 43.4 1.0 C B:SER18 3.5 47.2 1.0 CA B:SER306 4.0 43.4 1.0 CA B:ASP302 4.0 53.2 1.0 CB B:ASP302 4.2 54.5 1.0 N B:SER306 4.2 43.7 1.0 CA B:SER18 4.3 47.9 1.0 N B:ALA303 4.4 53.0 1.0 N B:LEU305 4.4 46.8 1.0 N B:PHE19 4.5 45.1 1.0 CA B:LEU305 4.6 45.2 1.0 CA B:ALA303 4.6 53.4 1.0 CB B:PHE19 4.6 41.5 1.0 CA B:PHE19 4.7 43.2 1.0 C B:ALA303 4.7 52.4 1.0 O B:HOH756 4.8 59.5 1.0 CB B:SER306 4.9 41.4 1.0 CG B:ASP302 4.9 56.2 1.0 N B:ASP304 5.0 51.1 1.0 O B:ALA303 5.0 52.2 1.0 C B:SER306 5.0 43.3 1.0

K.Manikandan, A.Bhardwaj, N.Gupta, N.K.Lokanath, A.Ghosh, V.S.Reddy, S.Ramakumar. Crystal Structures of Native and Xylosaccharide-Bound Alkali Thermostable Xylanase From An Alkalophilic Bacillus Sp. Ng-27: Structural Insights Into Alkalophilicity and Implications For Adaptation to Polyextreme Conditions. Protein Sci. V. 15 1951 2006.
ISSN: ISSN 0961-8368
PubMed: 16823036
DOI: 10.1110/PS.062220206