Magnesium in PDB 5ahk: Crystal Structure of Acetohydroxy Acid Synthase PF5 From Pseudomonas Protegens

All present enzymatic activity of Crystal Structure of Acetohydroxy Acid Synthase PF5 From Pseudomonas Protegens:
2.2.1.6;

The structure of Crystal Structure of Acetohydroxy Acid Synthase PF5 From Pseudomonas Protegens, PDB code: 5ahk was solved by D.Dobritzsch, S.Loschonsky, M.Mueller, G.Schneider, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	49.22 / 1.55
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	65.220, 139.870, 65.340, 90.00, 97.87, 90.00
R / Rfree (%)	15.11 / 17.39

The binding sites of Magnesium atom in the Crystal Structure of Acetohydroxy Acid Synthase PF5 From Pseudomonas Protegens (pdb code 5ahk). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of Acetohydroxy Acid Synthase PF5 From Pseudomonas Protegens, PDB code: 5ahk:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of Acetohydroxy Acid Synthase PF5 From Pseudomonas Protegens


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of Acetohydroxy Acid Synthase PF5 From Pseudomonas Protegens within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg702 b:12.9 occ:1.00 OD1 A:ASN473 2.1 13.7 1.0 OD1 A:ASP446 2.1 12.2 1.0 O3B A:TPP700 2.1 12.3 1.0 O1A A:TPP700 2.1 12.2 1.0 O A:SER475 2.1 13.9 1.0 O A:HOH2353 2.2 12.3 1.0 CG A:ASN473 3.0 13.9 1.0 CG A:ASP446 3.1 11.9 1.0 PB A:TPP700 3.2 11.8 1.0 PA A:TPP700 3.2 11.8 1.0 C A:SER475 3.4 15.1 1.0 O3A A:TPP700 3.4 11.8 1.0 ND2 A:ASN473 3.4 14.0 1.0 OD2 A:ASP446 3.6 12.4 1.0 O2B A:TPP700 3.8 11.8 1.0 O7 A:TPP700 4.0 12.6 1.0 N A:ASP446 4.0 11.3 1.0 N A:SER475 4.0 15.5 1.0 N A:GLY477 4.1 18.6 1.0 CA A:SER475 4.2 15.6 0.4 N A:ASN473 4.2 13.7 1.0 CA A:SER475 4.3 15.4 0.6 N A:LEU476 4.3 15.6 1.0 OG A:SER475 4.3 15.3 0.6 CB A:ASN473 4.4 14.2 1.0 CB A:ASP446 4.4 11.7 1.0 N A:GLY447 4.4 11.1 1.0 O2A A:TPP700 4.4 11.9 1.0 CA A:LEU476 4.4 15.8 1.0 O A:MET471 4.4 14.1 1.0 O1B A:TPP700 4.5 12.3 1.0 CA A:ASP446 4.6 11.3 1.0 CA A:ASN473 4.6 14.4 1.0 CA A:GLY445 4.7 10.9 1.0 C A:ASN473 4.7 14.9 1.0 N A:HIS474 4.8 15.5 1.0 C A:GLY445 4.8 11.1 1.0 CA A:GLY477 4.8 21.2 1.0 C A:LEU476 4.8 17.1 1.0 CB A:SER475 4.9 16.1 0.4 CB A:SER475 4.9 15.7 0.6 O A:HOH2356 4.9 15.9 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of Acetohydroxy Acid Synthase PF5 From Pseudomonas Protegens


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of Acetohydroxy Acid Synthase PF5 From Pseudomonas Protegens within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg702 b:12.7 occ:1.00 O B:SER475 2.1 14.0 1.0 OD1 B:ASN473 2.1 13.4 1.0 O3B B:TPP700 2.1 11.8 1.0 OD1 B:ASP446 2.1 12.3 1.0 O1A B:TPP700 2.2 11.4 1.0 O B:HOH2391 2.2 12.0 1.0 CG B:ASN473 3.1 13.9 1.0 CG B:ASP446 3.1 12.2 1.0 PA B:TPP700 3.2 11.6 1.0 PB B:TPP700 3.3 11.4 1.0 C B:SER475 3.3 15.8 1.0 O3A B:TPP700 3.4 11.0 1.0 ND2 B:ASN473 3.4 14.1 1.0 OD2 B:ASP446 3.6 12.5 1.0 O2B B:TPP700 3.8 11.4 1.0 O7 B:TPP700 4.0 11.8 1.0 N B:ASP446 4.0 11.6 1.0 N B:SER475 4.0 16.7 1.0 N B:GLY477 4.0 19.4 1.0 CA B:SER475 4.2 16.6 0.5 CA B:SER475 4.2 16.2 0.5 N B:ASN473 4.3 13.6 1.0 N B:LEU476 4.3 16.1 1.0 OG B:SER475 4.3 16.2 0.5 CB B:ASN473 4.4 14.4 1.0 CA B:LEU476 4.4 16.4 1.0 N B:GLY447 4.4 11.5 1.0 CB B:ASP446 4.4 12.1 1.0 O B:MET471 4.4 12.8 1.0 O1B B:TPP700 4.4 10.7 1.0 O2A B:TPP700 4.5 11.3 1.0 CA B:ASP446 4.6 11.7 1.0 CA B:ASN473 4.7 14.6 1.0 CA B:GLY445 4.7 11.2 1.0 C B:ASN473 4.7 15.1 1.0 N B:HIS474 4.7 15.7 1.0 CA B:GLY477 4.8 21.1 1.0 C B:GLY445 4.8 11.3 1.0 C B:LEU476 4.8 17.6 1.0 CB B:SER475 4.8 17.5 0.5 CB B:SER475 4.9 16.6 0.5

D.Dobritzsch, S.Loschonsky, M.Mueller, G.Schneider. The Crystal Structure of the Acetohydroxy Acid Synthase PF5 From Pseudomonas Protegens To Be Published.