Atomistry » Magnesium » PDB 8ijl-8iri » 8io8
Atomistry »
  Magnesium »
    PDB 8ijl-8iri »
      8io8 »

Magnesium in PDB 8io8: Cryo-Em Structure of Cyanobacteria Phosphoketolase Complexed with Amppnpin Dimeric Assembly

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Cryo-Em Structure of Cyanobacteria Phosphoketolase Complexed with Amppnpin Dimeric Assembly (pdb code 8io8). 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 Complexed with Amppnpin Dimeric Assembly, PDB code: 8io8:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 8io8

Go back to Magnesium Binding Sites List in 8io8
Magnesium binding site 1 out of 2 in the Cryo-Em Structure of Cyanobacteria Phosphoketolase Complexed with Amppnpin Dimeric Assembly


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 Complexed with Amppnpin Dimeric Assembly within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg803

b:76.9
occ:1.00
OD1 A:ASP178 2.1 73.3 1.0
O1A A:TPP802 2.1 82.0 1.0
O A:TYR213 2.1 78.9 1.0
O2B A:TPP802 2.1 82.0 1.0
OD1 A:ASN211 2.1 72.3 1.0
CG A:ASN211 3.0 72.3 1.0
CG A:ASP178 3.0 73.3 1.0
PB A:TPP802 3.2 82.0 1.0
ND2 A:ASN211 3.2 72.3 1.0
C A:TYR213 3.3 78.9 1.0
PA A:TPP802 3.3 82.0 1.0
OD2 A:ASP178 3.4 73.3 1.0
O3A A:TPP802 3.4 82.0 1.0
O3B A:TPP802 3.6 82.0 1.0
N A:TYR213 4.0 78.9 1.0
N A:ASP178 4.0 73.3 1.0
N A:GLY179 4.1 73.4 1.0
CA A:LYS214 4.1 80.8 1.0
N A:LYS214 4.1 80.8 1.0
O7 A:TPP802 4.2 82.0 1.0
NZ A:LYS293 4.3 74.8 1.0
CA A:TYR213 4.3 78.9 1.0
O A:HIS209 4.3 66.5 1.0
CB A:ASP178 4.4 73.3 1.0
CG2 A:THR219 4.4 77.6 1.0
CB A:ASN211 4.4 72.3 1.0
O2A A:TPP802 4.4 82.0 1.0
O1B A:TPP802 4.5 82.0 1.0
N A:ASN211 4.5 72.3 1.0
CA A:ASP178 4.6 73.3 1.0
N A:GLY212 4.7 74.8 1.0
C A:ASP178 4.8 73.3 1.0
CE A:LYS293 4.8 74.8 1.0
CA A:ASN211 4.8 72.3 1.0
CD A:LYS293 4.8 74.8 1.0
CB A:LYS214 4.9 80.8 1.0
C A:GLY177 4.9 68.9 1.0
C A:ASN211 4.9 72.3 1.0
CA A:GLY179 5.0 73.4 1.0
CA A:GLY177 5.0 68.9 1.0

Magnesium binding site 2 out of 2 in 8io8

Go back to Magnesium Binding Sites List in 8io8
Magnesium binding site 2 out of 2 in the Cryo-Em Structure of Cyanobacteria Phosphoketolase Complexed with Amppnpin Dimeric Assembly


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 Complexed with Amppnpin Dimeric Assembly within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg803

b:76.6
occ:1.00
OD1 B:ASP178 2.0 74.0 1.0
O B:TYR213 2.0 78.8 1.0
O3B B:TPP802 2.0 83.2 1.0
OD1 B:ASN211 2.2 72.3 1.0
O2A B:TPP802 2.4 83.2 1.0
PB B:TPP802 2.8 83.2 1.0
CG B:ASP178 3.0 74.0 1.0
O2B B:TPP802 3.1 83.2 1.0
CG B:ASN211 3.1 72.3 1.0
C B:TYR213 3.2 78.8 1.0
O3A B:TPP802 3.2 83.2 1.0
ND2 B:ASN211 3.3 72.3 1.0
OD2 B:ASP178 3.3 74.0 1.0
PA B:TPP802 3.4 83.2 1.0
CA B:LYS214 4.0 81.7 1.0
N B:LYS214 4.0 81.7 1.0
N B:TYR213 4.1 78.8 1.0
N B:ASP178 4.1 74.0 1.0
N B:GLY179 4.1 74.2 1.0
NZ B:LYS293 4.2 73.9 1.0
O1B B:TPP802 4.3 83.2 1.0
CA B:TYR213 4.3 78.8 1.0
CB B:ASP178 4.4 74.0 1.0
O7 B:TPP802 4.4 83.2 1.0
CG2 B:THR219 4.4 77.8 1.0
O1A B:TPP802 4.5 83.2 1.0
O B:HIS209 4.5 66.9 1.0
CB B:ASN211 4.5 72.3 1.0
CE B:LYS293 4.7 73.9 1.0
CA B:ASP178 4.7 74.0 1.0
N B:ASN211 4.7 72.3 1.0
N B:GLY212 4.8 75.4 1.0
CB B:LYS214 4.8 81.7 1.0
CD B:LYS293 4.8 73.9 1.0
C B:ASP178 4.9 74.0 1.0
CA B:ASN211 5.0 72.3 1.0
O B:LYS214 5.0 81.7 1.0
C B:GLY177 5.0 69.6 1.0

Reference:

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
Page generated: Fri Oct 4 09:29:44 2024

Last articles

Fe in 2YXO
Fe in 2YRS
Fe in 2YXC
Fe in 2YNM
Fe in 2YVJ
Fe in 2YP1
Fe in 2YU2
Fe in 2YU1
Fe in 2YQB
Fe in 2YOO
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy