Magnesium in PDB 3ahj: H553A Mutant of Phosphoketolase From Bifidobacterium Breve

All present enzymatic activity of H553A Mutant of Phosphoketolase From Bifidobacterium Breve:
4.1.2.22;

The structure of H553A Mutant of Phosphoketolase From Bifidobacterium Breve, PDB code: 3ahj was solved by R.Suzuki, T.Katayama, B.-J.Kim, T.Wakagi, H.Shoun, H.Ashida, K.Yamamoto, S.Fushinobu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	38.61 / 2.10
Space group	I 4 2 2
Cell size a, b, c (Å), α, β, γ (°)	175.077, 175.077, 163.996, 90.00, 90.00, 90.00
R / Rfree (%)	15.8 / 19.1

The binding sites of Magnesium atom in the H553A Mutant of Phosphoketolase From Bifidobacterium Breve (pdb code 3ahj). 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 H553A Mutant of Phosphoketolase From Bifidobacterium Breve, PDB code: 3ahj:

Magnesium binding site 1 out of 1 in the H553A Mutant of Phosphoketolase From Bifidobacterium Breve


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of H553A Mutant of Phosphoketolase From Bifidobacterium Breve within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg826 b:23.1 occ:1.00 O2A A:TPP827 1.9 23.9 1.0 O1B A:TPP827 2.0 22.4 1.0 OD1 A:ASP182 2.1 21.1 1.0 O A:HOH1189 2.2 19.5 1.0 O A:TYR217 2.2 23.1 1.0 OD1 A:ASN215 2.2 22.1 1.0 CG A:ASN215 3.1 23.6 1.0 PB A:TPP827 3.1 22.6 1.0 PA A:TPP827 3.1 23.4 1.0 CG A:ASP182 3.2 21.3 1.0 ND2 A:ASN215 3.4 25.0 1.0 C A:TYR217 3.4 23.3 1.0 O3A A:TPP827 3.4 20.2 1.0 O3B A:TPP827 3.6 21.9 1.0 OD2 A:ASP182 3.9 19.1 1.0 N A:ASP182 3.9 20.5 1.0 N A:GLY183 4.1 20.6 1.0 O7 A:TPP827 4.1 25.0 1.0 N A:TYR217 4.1 20.8 1.0 O A:HIS213 4.2 21.3 1.0 O1A A:TPP827 4.2 22.0 1.0 NZ A:LYS300 4.3 21.2 1.0 N A:LYS218 4.3 23.5 1.0 CA A:LYS218 4.4 21.1 1.0 CA A:TYR217 4.4 22.3 1.0 CB A:ASP182 4.4 17.8 1.0 CG2 A:THR223 4.5 18.9 1.0 CA A:ASP182 4.5 20.6 1.0 CB A:ASN215 4.5 21.7 1.0 O2B A:TPP827 4.5 24.5 1.0 N A:ASN215 4.6 22.1 1.0 CD A:LYS300 4.7 18.7 1.0 C A:ASP182 4.7 20.2 1.0 CA A:ASN215 4.8 21.8 1.0 N A:GLY216 4.9 20.9 1.0 C A:GLY181 4.9 21.4 1.0 C A:ASN215 4.9 20.5 1.0 CE A:LYS300 5.0 21.4 1.0

R.Suzuki, T.Katayama, B.-J.Kim, T.Wakagi, H.Shoun, H.Ashida, K.Yamamoto, S.Fushinobu. Crystal Structures of Phosphoketolase: Thiamine Diphosphate-Dependent Dehydration Mechanism J.Biol.Chem. V. 285 34279 2010.
ISSN: ISSN 0021-9258
PubMed: 20739284
DOI: 10.1074/JBC.M110.156281