Magnesium in PDB 1shk: The Three-Dimensional Structure of Shikimate Kinase From Erwinia Chrysanthemi

All present enzymatic activity of The Three-Dimensional Structure of Shikimate Kinase From Erwinia Chrysanthemi:
2.7.1.71;

The structure of The Three-Dimensional Structure of Shikimate Kinase From Erwinia Chrysanthemi, PDB code: 1shk was solved by T.Krell, J.R.Coggins, A.J.Lapthorn, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 1.90
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	108.500, 108.500, 92.800, 90.00, 90.00, 90.00
R / Rfree (%)	17.4 / 22.2

The binding sites of Magnesium atom in the The Three-Dimensional Structure of Shikimate Kinase From Erwinia Chrysanthemi (pdb code 1shk). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 3 binding sites of Magnesium where determined in the The Three-Dimensional Structure of Shikimate Kinase From Erwinia Chrysanthemi, PDB code: 1shk:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in the The Three-Dimensional Structure of Shikimate Kinase From Erwinia Chrysanthemi


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of The Three-Dimensional Structure of Shikimate Kinase From Erwinia Chrysanthemi within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg902 b:37.6 occ:1.00 O A:GLN144 2.3 35.1 1.0 O A:HOH1027 2.3 33.8 1.0 O A:ALA147 2.3 31.7 1.0 O A:HOH995 2.4 44.6 1.0 O A:HOH1026 2.4 32.5 1.0 C A:ALA147 3.4 33.3 1.0 C A:GLN144 3.5 34.0 1.0 N A:ALA147 3.9 30.6 1.0 O A:ASP145 4.0 33.6 1.0 CA A:ALA147 4.0 33.0 1.0 O A:HOH937 4.0 43.1 1.0 CB A:ALA147 4.1 33.3 1.0 C A:ASP145 4.2 34.6 1.0 NH1 A:ARG92 4.3 31.8 1.0 CA A:GLN144 4.3 34.4 1.0 N A:ASP145 4.4 32.9 1.0 CA A:ASP145 4.4 33.8 1.0 N A:HIS148 4.5 30.3 1.0 C A:VAL146 4.7 32.4 1.0 CA A:HIS148 4.8 30.5 1.0 N A:VAL146 4.8 32.5 1.0 OE1 A:GLN144 4.9 43.7 1.0 CB A:GLN144 5.0 36.6 1.0

Magnesium binding site 2 out of 3 in the The Three-Dimensional Structure of Shikimate Kinase From Erwinia Chrysanthemi


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of The Three-Dimensional Structure of Shikimate Kinase From Erwinia Chrysanthemi within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg903 b:34.8 occ:1.00 O A:ARG92 2.2 35.6 1.0 O A:GLY95 2.4 34.6 1.0 O A:ALA93 2.6 34.3 1.0 C A:GLY95 3.3 35.2 1.0 C A:ARG92 3.3 37.7 1.0 C A:ALA93 3.3 40.1 1.0 N A:GLY95 3.5 36.1 1.0 CA A:GLY95 3.7 36.7 1.0 CA A:ALA93 3.9 39.2 1.0 N A:ALA93 4.1 38.8 1.0 C A:HIS94 4.1 37.6 1.0 N A:HIS94 4.2 38.5 1.0 CA A:ARG92 4.4 38.6 1.0 N A:THR96 4.5 34.5 1.0 CE1 A:HIS148 4.6 34.0 1.0 O A:MET91 4.6 38.9 1.0 O A:HIS94 4.6 37.0 1.0 CA A:HIS94 4.7 38.4 1.0 OG1 A:THR96 4.8 31.3 1.0

Magnesium binding site 3 out of 3 in the The Three-Dimensional Structure of Shikimate Kinase From Erwinia Chrysanthemi


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of The Three-Dimensional Structure of Shikimate Kinase From Erwinia Chrysanthemi within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg901 b:34.3 occ:1.00 O B:GLN144 2.2 32.5 1.0 O B:HOH958 2.3 42.6 1.0 O B:ALA147 2.3 30.6 1.0 O B:HOH954 2.3 34.5 1.0 O B:HOH955 2.4 34.4 1.0 C B:GLN144 3.4 34.8 1.0 C B:ALA147 3.5 32.5 1.0 O B:HOH994 3.9 47.4 1.0 N B:ALA147 4.0 32.2 1.0 CA B:ALA147 4.1 30.7 1.0 O B:ASP145 4.1 29.9 1.0 C B:ASP145 4.2 28.2 1.0 CB B:ALA147 4.2 33.9 1.0 CA B:GLN144 4.3 33.4 1.0 NH1 B:ARG92 4.3 30.1 1.0 CA B:ASP145 4.4 31.3 1.0 N B:ASP145 4.4 32.9 1.0 N B:HIS148 4.6 32.8 1.0 OE1 B:GLN144 4.7 35.8 1.0 C B:VAL146 4.7 30.9 1.0 CA B:HIS148 4.8 32.4 1.0 N B:VAL146 4.8 29.6 1.0 CB B:GLN144 4.9 35.1 1.0 O B:HOH1035 5.0 64.3 1.0

T.Krell, J.E.Coyle, M.J.Horsburgh, J.R.Coggins, A.J.Lapthorn. Crystallization and Preliminary X-Ray Crystallographic Analysis of Shikimate Kinase From Erwinia Chrysanthemi. Acta Crystallogr.,Sect.D V. 53 612 1997.
ISSN: ISSN 0907-4449
PubMed: 15299895
DOI: 10.1107/S0907444997004319