Magnesium in PDB 5zt1: Structure of the Bacterial Pathogens Atpase with Substrate Atp Gamma S

All present enzymatic activity of Structure of the Bacterial Pathogens Atpase with Substrate Atp Gamma S:
3.6.3.14;

The structure of Structure of the Bacterial Pathogens Atpase with Substrate Atp Gamma S, PDB code: 5zt1 was solved by X.P.Gao, Z.X.Mu, S.Cui, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.87 / 3.11
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	104.267, 104.267, 145.769, 90.00, 90.00, 120.00
R / Rfree (%)	19.2 / 25.5

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 20; Page 3, Binding sites: 21 - 29;

Binding sites:

The binding sites of Magnesium atom in the Structure of the Bacterial Pathogens Atpase with Substrate Atp Gamma S (pdb code 5zt1). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 29 binding sites of Magnesium where determined in the Structure of the Bacterial Pathogens Atpase with Substrate Atp Gamma S, PDB code: 5zt1:
Jump to Magnesium binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Magnesium binding site 1 out of 29 in the Structure of the Bacterial Pathogens Atpase with Substrate Atp Gamma S


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of the Bacterial Pathogens Atpase with Substrate Atp Gamma S within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg503 b:24.1 occ:0.00 OG1 B:THR299 2.2 23.4 1.0 H B:THR299 2.3 26.7 1.0 HG B:SER297 2.3 40.3 1.0 HG1 B:THR299 2.4 28.1 1.0 OG B:SER297 2.5 33.6 1.0 HG3 B:LYS243 2.6 35.4 1.0 N B:THR299 3.0 22.2 1.0 HG3 B:GLU151 3.0 40.2 1.0 O B:VAL244 3.1 21.5 1.0 CB B:THR299 3.3 16.3 1.0 HD2 B:PHE136 3.4 29.3 1.0 HB B:THR299 3.4 19.5 1.0 H B:VAL244 3.4 26.1 1.0 HE2 B:PHE136 3.5 26.8 1.0 CG B:LYS243 3.6 29.5 1.0 HB2 B:SER297 3.6 31.1 1.0 H B:GLY152 3.6 30.2 1.0 CB B:SER297 3.7 25.9 1.0 HA B:ILE298 3.7 16.5 1.0 N B:VAL244 3.7 21.7 1.0 CA B:THR299 3.8 18.5 1.0 HG2 B:LYS243 3.8 35.4 1.0 HA B:LYS243 3.8 31.1 1.0 C B:ILE298 3.8 15.1 1.0 HA B:GLU151 3.9 35.8 1.0 C B:VAL244 3.9 19.6 1.0 CG B:GLU151 4.0 33.5 1.0 CD2 B:PHE136 4.0 24.4 1.0 C B:SER297 4.0 21.8 1.0 CE2 B:PHE136 4.0 22.3 1.0 CA B:ILE298 4.1 13.7 1.0 C B:LYS243 4.1 23.0 1.0 HE3 B:LYS243 4.1 47.8 1.0 O B:SER297 4.1 18.9 1.0 N B:GLY152 4.2 25.2 1.0 N B:ILE298 4.2 18.8 1.0 HA B:THR299 4.3 22.2 1.0 CA B:LYS243 4.3 25.9 1.0 HB3 B:SER297 4.3 31.1 1.0 CB B:LYS243 4.4 23.7 1.0 CA B:VAL244 4.4 15.8 1.0 CA B:SER297 4.5 21.6 1.0 CA B:GLU151 4.5 29.8 1.0 CD B:GLU151 4.5 43.4 1.0 HD2 B:LYS243 4.5 38.1 1.0 HA2 B:GLY152 4.5 28.3 1.0 CD B:LYS243 4.5 31.7 1.0 HB2 B:LYS243 4.5 28.4 1.0 HG2 B:GLU151 4.5 40.2 1.0 CG2 B:THR299 4.6 12.4 1.0 OE2 B:GLU151 4.6 39.9 1.0 HB2 B:GLU151 4.6 36.0 1.0 HA B:ALA245 4.6 19.4 1.0 CB B:GLU151 4.6 30.0 1.0 C B:GLU151 4.7 25.7 1.0 H B:ILE298 4.7 22.6 1.0 HG21 B:THR299 4.7 14.9 1.0 N B:ALA245 4.7 18.2 1.0 O B:ILE298 4.8 16.0 1.0 O B:LYS243 4.8 19.1 1.0 CE B:LYS243 4.8 39.9 1.0 HG23 B:THR299 4.8 14.9 1.0 CA B:GLY152 4.9 23.6 1.0 C B:THR299 4.9 17.3 1.0

Magnesium binding site 2 out of 29 in the Structure of the Bacterial Pathogens Atpase with Substrate Atp Gamma S


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Structure of the Bacterial Pathogens Atpase with Substrate Atp Gamma S within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg504 b:39.0 occ:0.00 H B:LYS165 1.9 49.8 1.0 HB2 B:LYS165 2.1 43.4 1.0 HB3 B:LYS165 2.5 43.4 1.0 O4 B:SO4501 2.6 38.1 0.0 CB B:LYS165 2.7 36.2 1.0 N B:LYS165 2.7 41.5 1.0 O B:SER160 2.7 37.2 1.0 C B:GLY162 3.2 44.2 1.0 N B:GLY162 3.3 50.5 1.0 CA B:LYS165 3.3 25.2 1.0 O B:GLY162 3.3 36.5 1.0 H B:GLY162 3.4 60.6 1.0 HB1 B:ALA159 3.5 25.0 1.0 HA3 B:GLY162 3.5 60.2 1.0 CA B:GLY162 3.5 50.1 1.0 C B:ALA161 3.6 43.7 1.0 HA B:ALA161 3.7 49.8 1.0 MG B:MG505 3.8 41.4 0.0 HA3 B:GLY164 3.8 40.9 1.0 C B:GLY164 3.8 30.2 1.0 N B:CYS163 3.8 46.9 1.0 HA B:LYS165 3.8 30.2 1.0 H B:GLY164 3.8 47.5 1.0 N B:GLY164 3.9 39.6 1.0 C B:SER160 3.9 34.4 1.0 HZ3 B:LYS165 3.9 70.4 1.0 CG B:LYS165 4.0 34.2 1.0 HE2 B:LYS165 4.0 57.6 1.0 HG3 B:LYS165 4.0 41.0 1.0 S B:SO4501 4.0 36.7 0.0 C B:CYS163 4.0 33.1 1.0 CA B:GLY164 4.0 34.0 1.0 CA B:ALA161 4.1 41.5 1.0 H B:THR166 4.1 33.6 1.0 O B:ALA161 4.1 36.9 1.0 HB3 B:ALA159 4.1 25.0 1.0 H B:CYS163 4.2 56.2 1.0 CB B:ALA159 4.2 20.9 1.0 O B:CYS163 4.3 33.3 1.0 N B:ALA161 4.4 50.1 1.0 C B:LYS165 4.5 24.6 1.0 HA2 B:GLY162 4.5 60.2 1.0 CA B:CYS163 4.5 38.3 1.0 O2 B:SO4501 4.6 32.9 0.0 N B:THR166 4.6 28.0 1.0 NZ B:LYS165 4.6 58.7 1.0 CE B:LYS165 4.6 48.0 1.0 HG2 B:LYS165 4.6 41.0 1.0 HD12 B:LEU329 4.6 29.5 1.0 O3 B:SO4501 4.6 34.6 0.0 HD13 B:LEU329 4.7 29.5 1.0 HG B:SER160 4.8 61.4 1.0 HZ1 B:LYS165 4.8 70.4 1.0 HB2 B:ALA159 4.8 25.0 1.0 HG23 B:THR166 4.8 37.9 1.0 CD B:LYS165 4.8 55.0 1.0 HA B:CYS163 4.9 46.0 1.0 O B:GLY164 4.9 22.6 1.0 O1 B:SO4501 4.9 38.0 0.0

Magnesium binding site 3 out of 29 in the Structure of the Bacterial Pathogens Atpase with Substrate Atp Gamma S


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Structure of the Bacterial Pathogens Atpase with Substrate Atp Gamma S within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg505 b:41.4 occ:0.00 O4 B:SO4501 2.5 38.1 0.0 O1 B:SO4501 2.7 38.0 0.0 HA3 B:GLY162 2.7 60.2 1.0 H B:GLY164 3.0 47.5 1.0 S B:SO4501 3.2 36.7 0.0 H B:CYS163 3.3 56.2 1.0 O B:ALA161 3.4 36.9 1.0 CA B:GLY162 3.6 50.1 1.0 N B:CYS163 3.8 46.9 1.0 N B:GLY164 3.8 39.6 1.0 MG B:MG504 3.8 39.0 0.0 HA3 B:GLY164 3.8 40.9 1.0 C B:ALA161 4.1 43.7 1.0 C B:GLY162 4.1 44.2 1.0 HG B:SER160 4.1 61.4 1.0 O3 B:SO4501 4.1 34.6 0.0 O2 B:SO4501 4.2 32.9 0.0 N B:GLY162 4.2 50.5 1.0 HA2 B:GLY162 4.3 60.2 1.0 CA B:GLY164 4.3 34.0 1.0 H B:LYS165 4.4 49.8 1.0 HB1 B:ALA334 4.5 42.1 1.0 O B:SER160 4.5 37.2 1.0 C B:CYS163 4.7 33.1 1.0 HB2 B:CYS163 4.7 51.4 1.0 CA B:CYS163 4.7 38.3 1.0 OG B:SER160 4.9 51.2 1.0 HB3 B:ALA334 5.0 42.1 1.0 H B:GLY162 5.0 60.6 1.0 HA2 B:GLY164 5.0 40.9 1.0

Magnesium binding site 4 out of 29 in the Structure of the Bacterial Pathogens Atpase with Substrate Atp Gamma S


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Structure of the Bacterial Pathogens Atpase with Substrate Atp Gamma S within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg506 b:15.9 occ:0.00 HH B:TYR302 1.5 13.8 1.0 OH B:TYR302 2.2 11.5 1.0 HG23 B:THR231 2.9 24.5 1.0 O B:LEU285 2.9 14.0 1.0 HG21 B:THR231 3.0 24.5 1.0 HD3 B:PRO289 3.1 16.1 1.0 HE1 B:TYR302 3.1 22.3 1.0 HG B:LEU285 3.2 17.9 1.0 OG1 B:THR231 3.3 19.5 1.0 CZ B:TYR302 3.3 11.4 1.0 CG2 B:THR231 3.3 20.4 1.0 HD21 B:LEU246 3.4 14.9 1.0 HD23 B:LEU246 3.4 14.9 1.0 CE1 B:TYR302 3.6 18.6 1.0 HD2 B:PRO289 3.7 16.1 1.0 HA B:LEU286 3.7 15.6 1.0 HD11 B:LEU285 3.7 16.4 1.0 CD B:PRO289 3.8 13.4 1.0 HB2 B:ARG288 3.8 33.3 1.0 CD2 B:LEU246 3.8 12.4 1.0 HD12 B:LEU285 3.8 16.4 1.0 C B:LEU285 3.9 14.9 1.0 HG3 B:PRO289 3.9 18.3 1.0 HD23 B:LEU286 4.0 12.7 1.0 CG B:LEU285 4.0 14.9 1.0 CB B:THR231 4.0 15.3 1.0 HG1 B:THR231 4.0 23.4 1.0 CD1 B:LEU285 4.1 13.6 1.0 HG22 B:THR231 4.2 24.5 1.0 HD22 B:LEU246 4.2 14.9 1.0 HD3 B:ARG288 4.3 25.3 1.0 CG B:PRO289 4.4 15.3 1.0 HG13 B:ILE248 4.4 8.0 1.0 CA B:LEU286 4.5 13.0 1.0 HD21 B:LEU285 4.5 16.1 1.0 H B:ARG288 4.5 19.7 1.0 CE2 B:TYR302 4.6 9.5 1.0 N B:LEU286 4.6 16.9 1.0 HB B:THR231 4.6 18.4 1.0 HA B:LEU285 4.6 22.3 1.0 CB B:ARG288 4.7 27.8 1.0 HA B:THR231 4.8 20.4 1.0 HD11 B:ILE248 4.8 9.5 1.0 CA B:LEU285 4.8 18.6 1.0 CD2 B:LEU285 4.8 13.4 1.0 HE2 B:TYR302 4.8 11.4 1.0 HG2 B:PRO289 4.9 18.3 1.0 HB1 B:ALA300 4.9 12.2 1.0 HG12 B:ILE248 4.9 8.0 1.0 CD2 B:LEU286 4.9 10.6 1.0

Magnesium binding site 5 out of 29 in the Structure of the Bacterial Pathogens Atpase with Substrate Atp Gamma S


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 5 of Structure of the Bacterial Pathogens Atpase with Substrate Atp Gamma S within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg507 b:32.3 occ:0.00 HH22 B:ARG154 2.3 44.9 1.0 H A:SER127 2.3 47.0 1.0 OE2 B:GLU287 2.3 41.1 1.0 HH12 B:ARG154 2.3 34.3 1.0 O B:ILE322 2.9 27.1 1.0 HG23 B:ILE322 2.9 45.0 1.0 HB3 A:SER127 2.9 36.1 1.0 HG2 B:GLU287 3.0 40.3 1.0 HB3 A:LEU125 3.0 39.8 1.0 NH2 B:ARG154 3.0 37.4 1.0 N A:SER127 3.0 39.2 1.0 NH1 B:ARG154 3.1 28.6 1.0 HB3 A:TYR126 3.2 35.4 1.0 H A:TYR126 3.3 32.1 1.0 CD B:GLU287 3.3 38.1 1.0 CG B:GLU287 3.4 33.6 1.0 HG3 B:GLU287 3.4 40.3 1.0 CZ B:ARG154 3.5 25.5 1.0 HG22 B:ILE322 3.5 45.0 1.0 N A:TYR126 3.6 26.8 1.0 HA B:ILE322 3.6 34.7 1.0 CB A:SER127 3.6 30.1 1.0 CG2 B:ILE322 3.6 37.5 1.0 OG A:SER127 3.7 29.4 1.0 HH21 B:ARG154 3.7 44.9 1.0 HH11 B:ARG154 3.8 34.3 1.0 HG A:SER127 3.9 35.2 1.0 C B:ILE322 3.9 26.7 1.0 CA A:SER127 3.9 32.1 1.0 C A:TYR126 3.9 35.5 1.0 CB A:LEU125 3.9 33.2 1.0 CB A:TYR126 4.0 29.5 1.0 CA A:TYR126 4.0 24.3 1.0 HG A:LEU125 4.0 32.4 1.0 CA B:ILE322 4.1 28.9 1.0 C A:LEU125 4.2 28.3 1.0 HD23 A:LEU125 4.2 37.2 1.0 HA A:SER127 4.3 38.5 1.0 HA A:LEU125 4.3 32.0 1.0 HG21 B:ILE322 4.3 45.0 1.0 CA A:LEU125 4.4 26.7 1.0 HB2 A:TYR126 4.4 35.4 1.0 OE1 B:GLU287 4.4 32.8 1.0 HB2 A:SER127 4.5 36.1 1.0 CG A:LEU125 4.5 27.0 1.0 CB B:ILE322 4.5 29.1 1.0 HB2 A:LEU125 4.5 39.8 1.0 HD2 A:TYR126 4.6 47.7 1.0 NE B:ARG154 4.7 19.4 1.0 HG12 B:ILE322 4.8 35.2 1.0 CD2 A:LEU125 4.8 31.0 1.0 H A:GLU128 4.9 37.6 1.0 CB B:GLU287 4.9 32.7 1.0 HA A:TYR126 5.0 29.2 1.0 O A:TYR126 5.0 32.5 1.0 HA B:GLU287 5.0 29.5 1.0 O A:LEU125 5.0 26.6 1.0

Magnesium binding site 6 out of 29 in the Structure of the Bacterial Pathogens Atpase with Substrate Atp Gamma S


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 6 of Structure of the Bacterial Pathogens Atpase with Substrate Atp Gamma S within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg508 b:33.2 occ:0.00 H B:SER160 2.0 39.4 1.0 O2 B:SO4501 2.5 32.9 0.0 OG B:SER160 2.7 51.2 1.0 N B:SER160 2.8 32.8 1.0 HG2 B:ARG331 3.0 55.5 1.0 HA B:ALA159 3.0 24.0 1.0 O B:LEU329 3.1 25.2 1.0 HG B:SER160 3.1 61.4 1.0 HG3 B:ARG331 3.2 55.5 1.0 HD12 B:LEU306 3.3 19.3 1.0 HB3 B:SER160 3.5 49.3 1.0 CB B:SER160 3.5 41.1 1.0 CG B:ARG331 3.5 46.3 1.0 CA B:SER160 3.7 35.1 1.0 CA B:ALA159 3.7 20.0 1.0 C B:ALA159 3.7 23.3 1.0 H B:ARG331 3.8 39.7 1.0 HB2 B:LEU329 3.8 20.9 1.0 C B:LEU329 3.8 21.3 1.0 N B:ARG331 3.9 33.1 1.0 S B:SO4501 3.9 36.7 0.0 HB1 B:ALA159 4.0 25.0 1.0 CD1 B:LEU306 4.0 16.1 1.0 HD13 B:LEU306 4.1 19.3 1.0 C B:SER330 4.2 26.4 1.0 HA B:SER330 4.2 25.0 1.0 HA B:ARG331 4.3 35.7 1.0 HB3 B:LEU329 4.3 20.9 1.0 HD11 B:LEU306 4.3 19.3 1.0 N B:SER330 4.4 18.0 1.0 HB2 B:SER160 4.4 49.3 1.0 CB B:LEU329 4.4 17.4 1.0 CB B:ALA159 4.4 20.9 1.0 O B:SER160 4.4 37.2 1.0 HD2 B:ARG331 4.4 50.5 1.0 HA B:SER160 4.5 42.1 1.0 CA B:ARG331 4.5 29.8 1.0 CA B:SER330 4.5 20.9 1.0 O1 B:SO4501 4.5 38.0 0.0 C B:SER160 4.5 34.4 1.0 CD B:ARG331 4.5 42.1 1.0 O4 B:SO4501 4.6 38.1 0.0 HE B:ARG331 4.6 55.7 1.0 CB B:ARG331 4.6 41.5 1.0 HB2 B:LEU306 4.6 25.0 1.0 CA B:LEU329 4.7 22.9 1.0 HB2 B:ALA159 4.7 25.0 1.0 O B:SER330 4.8 25.2 1.0 O3 B:SO4501 4.8 34.6 0.0 O B:PHE158 4.8 20.8 1.0 N B:ALA159 4.9 20.2 1.0 O B:ALA159 4.9 25.5 1.0 H B:SER330 5.0 21.6 1.0

Magnesium binding site 7 out of 29 in the Structure of the Bacterial Pathogens Atpase with Substrate Atp Gamma S


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 7 of Structure of the Bacterial Pathogens Atpase with Substrate Atp Gamma S within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg509 b:40.1 occ:0.00 H B:GLU317 1.5 48.1 1.0 HB2 B:GLU317 2.0 56.5 1.0 N B:GLU317 2.3 40.0 1.0 CB B:GLU317 2.8 47.0 1.0 HG3 B:GLU317 2.8 64.4 1.0 O B:PRO314 2.9 38.2 1.0 O B:ASP313 2.9 40.5 1.0 HB3 B:ALA316 3.0 51.6 1.0 CA B:GLU317 3.1 35.4 1.0 HA B:ASP310 3.1 44.4 1.0 HA B:PRO314 3.2 48.7 1.0 C B:PRO314 3.3 38.4 1.0 CG B:GLU317 3.3 53.7 1.0 H B:ALA316 3.3 40.3 1.0 N B:ALA316 3.4 33.6 1.0 C B:ALA316 3.4 34.1 1.0 O B:ASP310 3.5 33.5 1.0 HB3 B:GLU317 3.6 56.5 1.0 HB3 B:ASP310 3.6 37.9 1.0 HA B:GLU317 3.7 42.5 1.0 CA B:ALA316 3.7 31.3 1.0 CA B:PRO314 3.7 40.6 1.0 CB B:ALA316 3.7 43.0 1.0 H B:GLU318 3.8 40.1 1.0 CA B:ASP310 3.8 37.0 1.0 C B:LEU315 3.9 35.1 1.0 OE2 B:GLU317 4.0 55.1 1.0 C B:ASP313 4.0 33.4 1.0 CB B:ASP310 4.0 31.6 1.0 OD1 B:ASP310 4.1 34.7 1.0 N B:LEU315 4.1 34.3 1.0 HG2 B:GLU317 4.1 64.4 1.0 CG B:ASP310 4.1 38.5 1.0 C B:ASP310 4.1 33.0 1.0 CD B:GLU317 4.2 51.2 1.0 C B:GLU317 4.2 30.6 1.0 HB1 B:ALA316 4.3 51.6 1.0 N B:GLU318 4.3 33.5 1.0 HB2 B:ALA316 4.3 51.6 1.0 N B:PRO314 4.4 25.6 1.0 O B:LEU315 4.5 33.8 1.0 O B:ALA316 4.5 36.9 1.0 H B:LEU315 4.6 41.2 1.0 CA B:LEU315 4.6 31.6 1.0 HA B:ALA316 4.6 37.6 1.0 OD2 B:ASP310 4.8 48.7 1.0 HB3 B:ASP313 4.9 56.4 1.0 HB2 B:ASP310 5.0 37.9 1.0 HH12 B:ARG320 5.0 39.1 1.0 HH22 B:ARG320 5.0 58.9 1.0

Magnesium binding site 8 out of 29 in the Structure of the Bacterial Pathogens Atpase with Substrate Atp Gamma S


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 8 of Structure of the Bacterial Pathogens Atpase with Substrate Atp Gamma S within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg510 b:30.5 occ:0.00 HD22 B:ASN170 1.8 32.1 1.0 ND2 B:ASN170 2.7 26.7 1.0 MG B:MG518 2.9 39.4 0.0 HB2 B:ASN170 3.0 30.7 1.0 HD21 B:ASN170 3.2 32.1 1.0 HB3 B:ASN170 3.2 30.7 1.0 CB B:ASN170 3.4 25.6 1.0 CG B:ASN170 3.5 19.4 1.0 HA B:PHE167 3.6 33.2 1.0 HD2 B:TYR412 3.8 41.2 1.0 HB2 B:TYR412 3.8 42.9 1.0 HE1 B:TYR199 4.0 34.3 1.0 HD2 B:PHE167 4.1 47.0 1.0 HD1 B:TYR199 4.2 30.1 1.0 CD2 B:TYR412 4.3 34.4 1.0 CA B:PHE167 4.5 27.6 1.0 CE1 B:TYR199 4.5 28.6 1.0 O B:THR166 4.6 23.1 1.0 CB B:TYR412 4.6 35.8 1.0 CD1 B:TYR199 4.6 25.1 1.0 O B:PHE167 4.7 21.3 1.0 OD1 B:ASN170 4.7 17.5 1.0 CG B:TYR412 4.7 32.9 1.0 CD2 B:PHE167 4.7 39.1 1.0 HB3 B:TYR412 4.8 42.9 1.0 CA B:ASN170 4.9 25.9 1.0 CE2 B:TYR412 5.0 36.0 1.0

Magnesium binding site 9 out of 29 in the Structure of the Bacterial Pathogens Atpase with Substrate Atp Gamma S


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 9 of Structure of the Bacterial Pathogens Atpase with Substrate Atp Gamma S within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg511 b:24.6 occ:0.00 HE B:ARG238 1.6 16.6 1.0 HH21 B:ARG238 2.1 23.2 1.0 NE B:ARG238 2.4 13.9 1.0 HB3 B:ARG238 2.6 32.1 1.0 NH2 B:ARG238 2.8 19.4 1.0 HG23 B:THR239 2.9 44.9 1.0 CZ B:ARG238 3.0 12.4 1.0 O B:GLU235 3.0 30.5 1.0 HA B:GLU235 3.0 24.2 1.0 HG22 B:THR239 3.1 44.9 1.0 HG2 B:GLU235 3.2 27.3 1.0 HB3 B:GLU235 3.3 28.3 1.0 HG2 B:ARG238 3.4 25.8 1.0 CB B:ARG238 3.4 26.7 1.0 CG2 B:THR239 3.5 37.4 1.0 CD B:ARG238 3.5 16.6 1.0 HH22 B:ARG238 3.6 23.2 1.0 CA B:GLU235 3.6 20.1 1.0 CG B:ARG238 3.6 21.5 1.0 C B:GLU235 3.7 23.9 1.0 CB B:GLU235 3.8 23.6 1.0 HD21 B:LEU292 3.8 25.7 1.0 HG21 B:THR239 3.8 44.9 1.0 H B:THR239 3.9 35.4 1.0 HD22 B:LEU292 3.9 25.7 1.0 HB2 B:ARG238 3.9 32.1 1.0 CG B:GLU235 3.9 22.8 1.0 HD3 B:ARG238 4.1 19.9 1.0 HD2 B:ARG238 4.1 19.9 1.0 N B:THR239 4.2 29.5 1.0 HD11 B:ILE298 4.2 16.1 1.0 CD2 B:LEU292 4.3 21.4 1.0 NH1 B:ARG238 4.3 13.6 1.0 HD12 B:ILE298 4.4 16.1 1.0 CA B:ARG238 4.5 32.8 1.0 C B:ARG238 4.5 28.4 1.0 H B:ARG238 4.5 31.5 1.0 HG3 B:ARG238 4.6 25.8 1.0 HG3 B:GLU235 4.6 27.3 1.0 HD23 B:LEU292 4.7 25.7 1.0 HB2 B:GLU235 4.7 28.3 1.0 HH11 B:ARG238 4.7 16.3 1.0 CD B:GLU235 4.8 30.4 1.0 CD1 B:ILE298 4.8 13.4 1.0 CB B:THR239 4.8 36.6 1.0 HH12 B:ARG238 4.9 16.3 1.0 CA B:THR239 4.9 37.3 1.0 N B:PHE236 4.9 32.7 1.0 HA B:THR239 5.0 44.8 1.0 N B:ARG238 5.0 26.2 1.0 HG3 B:PRO124 5.0 31.0 1.0 N B:GLU235 5.0 24.0 1.0

Magnesium binding site 10 out of 29 in the Structure of the Bacterial Pathogens Atpase with Substrate Atp Gamma S


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 10 of Structure of the Bacterial Pathogens Atpase with Substrate Atp Gamma S within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg512 b:38.0 occ:0.00 H B:VAL142 2.5 30.9 1.0 HB2 B:LYS141 2.6 40.2 1.0 OE1 B:GLN410 2.8 39.2 1.0 HG12 B:VAL142 2.8 46.1 1.0 HB2 B:GLN410 2.8 44.9 1.0 HG23 B:ILE140 3.1 23.2 1.0 O B:LEU408 3.1 42.5 1.0 HG22 B:ILE140 3.2 23.2 1.0 H B:LYS141 3.2 40.0 1.0 HE3 B:LYS141 3.2 49.1 1.0 N B:VAL142 3.3 25.8 1.0 HB B:VAL142 3.4 27.8 1.0 N B:LYS141 3.4 33.4 1.0 CB B:LYS141 3.5 33.5 1.0 HD2 B:PRO340 3.5 42.1 1.0 CG2 B:ILE140 3.6 19.3 1.0 CG1 B:VAL142 3.6 38.4 1.0 CB B:GLN410 3.7 37.4 1.0 HB3 B:GLN410 3.7 44.9 1.0 HG3 B:PRO340 3.8 43.1 1.0 CA B:LYS141 3.8 31.3 1.0 HG11 B:VAL142 3.8 46.1 1.0 CB B:VAL142 3.9 23.1 1.0 CD B:GLN410 3.9 38.2 1.0 HG2 B:PRO340 3.9 43.1 1.0 C B:LYS141 4.0 25.7 1.0 C B:LEU408 4.0 47.2 1.0 HB3 B:LYS141 4.0 40.2 1.0 C B:ILE140 4.0 29.1 1.0 HA B:LEU408 4.1 45.8 1.0 HA B:ILE140 4.1 36.1 1.0 CG B:PRO340 4.1 35.9 1.0 CD B:PRO340 4.2 35.1 1.0 HG3 B:LYS141 4.2 34.2 1.0 O B:PHE407 4.2 32.4 1.0 CE B:LYS141 4.2 41.0 1.0 CA B:VAL142 4.2 21.8 1.0 HG21 B:ILE140 4.2 23.2 1.0 CG B:LYS141 4.3 28.5 1.0 HG13 B:VAL142 4.4 46.1 1.0 CG B:GLN410 4.4 37.0 1.0 HD3 B:PRO340 4.4 42.1 1.0 CA B:ILE140 4.4 30.1 1.0 O B:LYS409 4.5 39.1 1.0 C B:LYS409 4.5 32.2 1.0 N B:GLN410 4.6 31.3 1.0 HE2 B:LYS141 4.6 49.1 1.0 CA B:LEU408 4.6 38.1 1.0 CB B:ILE140 4.6 24.3 1.0 CA B:GLN410 4.7 34.9 1.0 CD B:LYS141 4.7 39.9 1.0 HA B:VAL142 4.7 26.1 1.0 O B:ILE140 4.7 28.9 1.0 HA B:LYS141 4.8 37.6 1.0 HD2 B:LYS141 4.8 47.9 1.0 H B:GLN410 4.9 37.6 1.0 H B:ILE143 4.9 30.6 1.0 HG3 B:GLN410 4.9 44.5 1.0 N B:LYS409 5.0 42.1 1.0 HZ2 B:LYS141 5.0 44.2 1.0

X.Gao, Z.Mu, X.Yu, B.Qin, J.Wojdyla, M.Wang, S.Cui. Structural Insight Into Conformational Changes Induced By Atp Binding in A Type III Secretion-Associated Atpase Fromshigella Flexneri Front Microbiol V. 9 1468 2018.
ISSN: ESSN 1664-302X
PubMed: 30013545
DOI: 10.3389/FMICB.2018.01468