Magnesium in PDB 8ioa: Cryo-Em Structure of Cyanobacteria Phosphoketolase

The binding sites of Magnesium atom in the Cryo-Em Structure of Cyanobacteria Phosphoketolase (pdb code 8ioa). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Cryo-Em Structure of Cyanobacteria Phosphoketolase, PDB code: 8ioa:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Cryo-Em Structure of Cyanobacteria Phosphoketolase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Cryo-Em Structure of Cyanobacteria Phosphoketolase within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg801 b:120.5 occ:1.00 O3B A:TPP802 1.9 126.6 1.0 OD1 A:ASN211 2.1 113.6 1.0 OD1 A:ASP178 2.1 116.4 1.0 O A:TYR213 2.6 128.0 1.0 O2A A:TPP802 2.6 126.6 1.0 CG A:ASN211 2.8 113.6 1.0 PB A:TPP802 2.9 126.6 1.0 ND2 A:ASN211 2.9 113.6 1.0 CG A:ASP178 3.1 116.4 1.0 O2B A:TPP802 3.3 126.6 1.0 O3A A:TPP802 3.3 126.6 1.0 OD2 A:ASP178 3.4 116.4 1.0 PA A:TPP802 3.5 126.6 1.0 C A:TYR213 3.7 128.0 1.0 N A:ASP178 4.1 116.4 1.0 NZ A:LYS293 4.1 116.2 1.0 CG2 A:THR219 4.2 122.5 1.0 N A:GLY179 4.2 112.7 1.0 N A:TYR213 4.2 128.0 1.0 CE A:LYS293 4.2 116.2 1.0 O1B A:TPP802 4.2 126.6 1.0 CB A:ASN211 4.3 113.6 1.0 CB A:ASP178 4.5 116.4 1.0 O A:HIS209 4.5 103.9 1.0 O1A A:TPP802 4.5 126.6 1.0 N A:ASN211 4.6 113.6 1.0 N A:LYS214 4.6 129.7 1.0 CA A:TYR213 4.6 128.0 1.0 CA A:LYS214 4.6 129.7 1.0 O7 A:TPP802 4.7 126.6 1.0 N A:GLY212 4.7 121.0 1.0 CA A:ASP178 4.7 116.4 1.0 CA A:ASN211 4.9 113.6 1.0 C A:GLY177 4.9 108.2 1.0 C A:ASP178 5.0 116.4 1.0 CA A:GLY177 5.0 108.2 1.0

Magnesium binding site 2 out of 2 in the Cryo-Em Structure of Cyanobacteria Phosphoketolase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Cryo-Em Structure of Cyanobacteria Phosphoketolase within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg802 b:119.4 occ:1.00 O1A B:TPP801 2.1 126.4 1.0 O1B B:TPP801 2.1 126.4 1.0 OD1 B:ASN211 2.2 113.2 1.0 ND2 B:ASN211 2.3 113.2 1.0 OD1 B:ASP178 2.4 114.3 1.0 CG B:ASN211 2.6 113.2 1.0 PB B:TPP801 2.9 126.4 1.0 O2B B:TPP801 3.1 126.4 1.0 O B:TYR213 3.1 128.8 1.0 O3A B:TPP801 3.2 126.4 1.0 PA B:TPP801 3.2 126.4 1.0 CG B:ASP178 3.5 114.3 1.0 OD2 B:ASP178 4.0 114.3 1.0 CB B:ASN211 4.1 113.2 1.0 N B:ASP178 4.1 114.3 1.0 O7 B:TPP801 4.2 126.4 1.0 C B:TYR213 4.2 128.8 1.0 O2A B:TPP801 4.2 126.4 1.0 O B:HIS209 4.3 104.4 1.0 O3B B:TPP801 4.3 126.4 1.0 N B:GLY179 4.3 111.7 1.0 CE B:LYS293 4.5 118.6 1.0 N B:ASN211 4.6 113.2 1.0 CA B:GLY177 4.6 108.0 1.0 CG2 B:THR219 4.7 120.9 1.0 N B:TYR213 4.7 128.8 1.0 C B:GLY177 4.7 108.0 1.0 CB B:ASP178 4.8 114.3 1.0 CA B:ASN211 4.9 113.2 1.0 N B:GLY212 4.9 120.5 1.0 NZ B:LYS293 4.9 118.6 1.0 CA B:ASP178 4.9 114.3 1.0

C.-W.Chang, M.-D.Tsai. An Atp-Sensitive Phosphoketolase Regulates Carbon Fixation in Cyanobacteria. Nat Metab 2023.
ISSN: ISSN 2522-5812
DOI: 10.1038/S42255-023-00831-W