Magnesium in PDB 3ahf: Phosphoketolase From Bifidobacterium Breve Complexed with Inorganic Phosphate

All present enzymatic activity of Phosphoketolase From Bifidobacterium Breve Complexed with Inorganic Phosphate:
4.1.2.22;

The structure of Phosphoketolase From Bifidobacterium Breve Complexed with Inorganic Phosphate, PDB code: 3ahf 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)	40.88 / 2.30
Space group	I 4 2 2
Cell size a, b, c (Å), α, β, γ (°)	173.906, 173.906, 163.522, 90.00, 90.00, 90.00
R / Rfree (%)	17.7 / 22.6

The binding sites of Magnesium atom in the Phosphoketolase From Bifidobacterium Breve Complexed with Inorganic Phosphate (pdb code 3ahf). 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 Phosphoketolase From Bifidobacterium Breve Complexed with Inorganic Phosphate, PDB code: 3ahf:

Magnesium binding site 1 out of 1 in the Phosphoketolase From Bifidobacterium Breve Complexed with Inorganic Phosphate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Phosphoketolase From Bifidobacterium Breve Complexed with Inorganic Phosphate within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg827 b:21.1 occ:1.00 OD1 A:ASP182 2.0 20.3 1.0 O2A A:TPP826 2.1 24.4 1.0 O A:HOH1269 2.1 21.2 1.0 O1B A:TPP826 2.1 23.6 1.0 OD1 A:ASN215 2.2 20.8 1.0 O A:TYR217 2.3 18.5 1.0 CG A:ASN215 3.1 20.6 1.0 PB A:TPP826 3.1 21.9 1.0 PA A:TPP826 3.2 21.2 1.0 CG A:ASP182 3.2 22.0 1.0 O3A A:TPP826 3.3 19.4 1.0 ND2 A:ASN215 3.4 23.4 1.0 C A:TYR217 3.5 18.8 1.0 O3B A:TPP826 3.6 22.8 1.0 N A:ASP182 3.8 21.8 1.0 OD2 A:ASP182 3.9 19.7 1.0 N A:GLY183 4.0 20.9 1.0 O7 A:TPP826 4.1 23.8 1.0 N A:TYR217 4.1 19.2 1.0 O A:HIS213 4.1 20.9 1.0 CE A:LYS300 4.3 22.6 1.0 O1A A:TPP826 4.3 20.7 1.0 N A:LYS218 4.4 19.7 1.0 CB A:ASP182 4.4 20.7 1.0 CA A:TYR217 4.4 19.1 1.0 CA A:ASP182 4.4 21.5 1.0 NZ A:LYS300 4.5 16.9 1.0 CA A:LYS218 4.5 18.0 1.0 CB A:ASN215 4.5 19.1 1.0 CG2 A:THR223 4.5 13.9 1.0 N A:ASN215 4.5 19.9 1.0 O2B A:TPP826 4.5 23.4 1.0 C A:ASP182 4.7 21.7 1.0 N A:GLY216 4.8 19.3 1.0 C A:GLY181 4.8 21.6 1.0 CA A:ASN215 4.8 19.2 1.0 C A:ASN215 4.9 18.6 1.0 CA A:GLY183 4.9 19.4 1.0 CA A:GLY181 4.9 19.6 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