Magnesium in PDB 5ybi: Structure of the Bacterial Pathogens Atpase with Substrate Amppnp

All present enzymatic activity of Structure of the Bacterial Pathogens Atpase with Substrate Amppnp:
3.6.3.14;

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

Resolution Low / High (Å)	43.00 / 2.27
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	105.017, 105.017, 146.642, 90.00, 90.00, 120.00
R / Rfree (%)	17.9 / 22.7

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 20; Page 3, Binding sites: 21 - 30; Page 4, Binding sites: 31 - 38;

Binding sites:

The binding sites of Magnesium atom in the Structure of the Bacterial Pathogens Atpase with Substrate Amppnp (pdb code 5ybi). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 38 binding sites of Magnesium where determined in the Structure of the Bacterial Pathogens Atpase with Substrate Amppnp, PDB code: 5ybi:
Jump to Magnesium binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Magnesium binding site 1 out of 38 in the Structure of the Bacterial Pathogens Atpase with Substrate Amppnp


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 Amppnp within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg506 b:59.8 occ:1.00 HOB2 A:ANP505 1.6 50.9 0.7 O2B A:ANP505 2.4 42.4 0.7 O1G A:ANP505 2.5 54.5 0.7 O2A A:ANP505 2.6 51.9 0.7 HG1 A:THR166 2.6 41.5 1.0 O A:HOH683 2.6 32.4 1.0 OG1 A:THR166 2.7 34.6 1.0 N3B A:ANP505 3.1 44.2 0.7 HOG2 A:ANP505 3.1 65.1 0.7 HB A:THR166 3.2 46.7 1.0 PG A:ANP505 3.2 61.2 0.7 PB A:ANP505 3.3 37.9 0.7 O A:HOH622 3.4 36.6 1.0 CB A:THR166 3.4 38.9 1.0 O2G A:ANP505 3.6 54.2 0.7 HZ2 A:LYS165 3.6 45.0 1.0 HG21 A:THR166 3.8 39.6 1.0 PA A:ANP505 3.8 56.8 0.7 HNB1 A:ANP505 3.9 53.1 0.7 O3A A:ANP505 4.0 48.0 0.7 HZ1 A:LYS165 4.0 45.0 1.0 OE1 A:GLU195 4.1 57.1 1.0 HG2 A:GLU192 4.1 40.0 1.0 CG2 A:THR166 4.2 33.0 1.0 NZ A:LYS165 4.2 37.5 1.0 H A:THR166 4.3 45.4 1.0 OE2 A:GLU192 4.3 48.9 1.0 HZ3 A:LYS165 4.5 45.0 1.0 O1B A:ANP505 4.6 38.6 0.7 O1A A:ANP505 4.6 44.7 0.7 O3G A:ANP505 4.7 49.6 0.7 HG23 A:THR166 4.7 39.6 1.0 CA A:THR166 4.7 37.1 1.0 HOG3 A:ANP505 4.8 59.5 0.7 HG3 A:LYS165 4.8 53.5 1.0 N A:THR166 4.9 37.8 1.0 HG22 A:THR166 4.9 39.6 1.0 CG A:GLU192 4.9 33.3 1.0 HB3 A:GLU192 4.9 38.6 1.0

Magnesium binding site 2 out of 38 in the Structure of the Bacterial Pathogens Atpase with Substrate Amppnp


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 Amppnp within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg507 b:42.3 occ:1.00 HB3 A:ASP324 1.6 53.4 1.0 CB A:ASP324 2.3 44.5 1.0 HB2 A:ASP324 2.4 53.4 1.0 O B:HOH745 2.5 33.9 1.0 HZ2 B:LYS293 2.6 71.1 1.0 O B:HOH661 2.7 36.8 1.0 HA B:SER127 2.9 37.3 1.0 CG A:ASP324 3.0 34.2 1.0 OD2 A:ASP324 3.0 16.9 1.0 HZ1 B:LYS293 3.2 71.1 1.0 NZ B:LYS293 3.3 59.2 1.0 HB2 B:SER127 3.5 38.7 1.0 HB2 A:ARG350 3.5 36.6 1.0 CA A:ASP324 3.6 37.1 1.0 HA A:ASP324 3.6 44.5 1.0 HZ3 B:LYS293 3.7 71.1 1.0 HB3 A:ARG350 3.7 36.6 1.0 CA B:SER127 3.7 31.1 1.0 CB B:SER127 3.9 32.3 1.0 O B:SER127 4.0 32.9 1.0 HB3 B:SER127 4.0 38.7 1.0 OD1 A:ASP324 4.0 34.0 1.0 CB A:ARG350 4.1 30.5 1.0 HD2 A:ARG350 4.1 48.8 1.0 HD3 A:ARG350 4.1 48.8 1.0 HG13 A:VAL351 4.2 36.6 1.0 C B:SER127 4.3 39.7 1.0 HE3 B:LYS293 4.4 49.3 1.0 N A:ASP324 4.4 24.0 1.0 CE B:LYS293 4.5 41.1 1.0 HH21 A:ARG154 4.5 30.8 1.0 CD A:ARG350 4.5 40.7 1.0 HG12 A:VAL351 4.5 36.6 1.0 O A:LEU323 4.6 24.4 1.0 HE1 B:TYR126 4.6 61.3 1.0 C A:ASP324 4.6 24.8 1.0 HD1 B:TYR126 4.6 69.9 1.0 HH11 A:ARG350 4.6 53.4 1.0 O A:ASP324 4.7 29.6 1.0 O A:ARG350 4.8 31.2 1.0 HD2 B:LYS293 4.8 44.3 1.0 CG1 A:VAL351 4.8 30.5 1.0 N B:SER127 4.8 35.6 1.0 H A:ASP324 4.9 28.8 1.0 O A:HOH604 4.9 19.3 1.0 C A:LEU323 4.9 27.2 1.0 O B:TYR126 4.9 35.1 1.0 CG A:ARG350 4.9 33.8 1.0 C A:ARG350 5.0 28.5 1.0

Magnesium binding site 3 out of 38 in the Structure of the Bacterial Pathogens Atpase with Substrate Amppnp


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 Amppnp within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg508 b:49.1 occ:1.00 H A:SER220 2.6 33.0 1.0 HA A:SER219 3.3 35.8 1.0 HB2 A:SER219 3.4 33.6 1.0 O A:HOH729 3.4 26.6 1.0 N A:SER220 3.5 27.5 1.0 HB2 A:SER220 3.5 35.1 1.0 OG A:SER220 3.7 33.1 1.0 HG A:SER220 3.8 39.7 1.0 CA A:SER219 4.0 29.8 1.0 CB A:SER220 4.0 29.2 1.0 CB A:SER219 4.1 28.0 1.0 C A:SER219 4.3 28.2 1.0 O A:HOH747 4.4 45.2 1.0 CA A:SER220 4.4 22.9 1.0 HB3 A:SER219 4.4 33.6 1.0 H A:VAL221 4.9 29.3 1.0 HB3 A:ASP260 4.9 37.7 1.0 HA A:SER220 4.9 27.5 1.0 HB3 A:SER220 4.9 35.1 1.0

Magnesium binding site 4 out of 38 in the Structure of the Bacterial Pathogens Atpase with Substrate Amppnp


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 Amppnp within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg509 b:45.5 occ:1.00 O A:HOH739 2.2 38.5 1.0 HD22 A:LEU414 3.1 39.0 1.0 O A:GLY415 3.4 45.6 1.0 O A:HOH689 3.4 44.1 1.0 HB3 A:LEU414 3.7 50.8 1.0 O A:HOH637 4.0 43.4 1.0 CD2 A:LEU414 4.0 32.5 1.0 CE1 A:PHE416 4.1 40.4 1.0 CZ A:PHE416 4.2 38.8 1.0 HD23 A:LEU414 4.3 39.0 1.0 HE1 A:PHE416 4.3 48.4 1.0 H A:GLY415 4.3 55.5 1.0 HZ A:PHE416 4.4 46.5 1.0 HD13 A:LEU414 4.4 47.1 1.0 C A:GLY415 4.4 46.4 1.0 CD1 A:PHE416 4.4 42.6 1.0 HA A:PHE416 4.5 44.6 1.0 CE2 A:PHE416 4.5 43.4 1.0 CB A:LEU414 4.5 42.4 1.0 HD21 A:LEU414 4.6 39.0 1.0 HA A:LEU414 4.6 50.6 1.0 N A:GLY415 4.7 46.2 1.0 CG A:PHE416 4.8 41.1 1.0 HD1 A:PHE416 4.8 51.1 1.0 CG A:LEU414 4.8 41.5 1.0 CD2 A:PHE416 4.8 44.6 1.0 OE1 A:GLN420 4.8 38.5 1.0 HE2 A:PHE416 4.9 52.0 1.0

Magnesium binding site 5 out of 38 in the Structure of the Bacterial Pathogens Atpase with Substrate Amppnp


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 Amppnp within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg510 b:42.6 occ:1.00 H A:LYS291 2.1 36.0 1.0 N A:LYS291 2.9 30.0 1.0 HA2 A:GLY290 3.0 33.1 1.0 HG13 A:ILE132 3.2 34.6 1.0 HA3 A:GLY290 3.2 33.1 1.0 HB2 A:LYS291 3.2 42.6 1.0 O A:HOH671 3.3 30.4 1.0 CA A:GLY290 3.4 27.6 1.0 O A:ALA130 3.5 37.4 1.0 HD11 A:ILE132 3.6 34.4 1.0 HH11 A:ARG129 3.6 37.7 1.0 HA3 A:GLY152 3.6 28.9 1.0 C A:GLY290 3.6 28.0 1.0 HH B:TYR126 3.7 66.4 1.0 OH B:TYR126 3.7 55.4 1.0 O A:LYS291 3.7 31.4 1.0 HG12 A:ILE132 3.7 34.6 1.0 HB3 A:LYS291 3.8 42.6 1.0 CB A:LYS291 3.8 35.5 1.0 CA A:LYS291 3.8 33.7 1.0 HB3 A:ARG129 3.8 41.5 1.0 CG1 A:ILE132 3.8 28.8 1.0 O A:GLY152 3.9 23.9 1.0 HD3 A:ARG129 3.9 41.2 1.0 CZ B:TYR126 4.2 44.7 1.0 CD1 A:ILE132 4.2 28.7 1.0 C A:LYS291 4.2 26.6 1.0 CA A:GLY152 4.4 24.1 1.0 NH1 A:ARG129 4.4 31.4 1.0 C A:GLY152 4.4 22.4 1.0 HG2 A:ARG129 4.5 35.5 1.0 HD12 A:ILE132 4.6 34.4 1.0 HA2 A:GLY152 4.6 28.9 1.0 HH12 A:ARG129 4.6 37.7 1.0 HE2 B:TYR126 4.6 52.2 1.0 HA A:LYS291 4.6 40.4 1.0 CE2 B:TYR126 4.6 43.5 1.0 H A:ALA130 4.6 43.0 1.0 C A:ALA130 4.7 34.7 1.0 CB A:ARG129 4.7 34.6 1.0 CE1 B:TYR126 4.7 51.1 1.0 CD A:ARG129 4.8 34.3 1.0 HE1 B:TYR126 4.8 61.3 1.0 N A:GLY290 4.8 23.7 1.0 O A:GLY290 4.8 31.0 1.0 CG A:ARG129 4.9 29.6 1.0 H A:ILE132 4.9 47.7 1.0 HD13 A:ILE132 5.0 34.4 1.0

Magnesium binding site 6 out of 38 in the Structure of the Bacterial Pathogens Atpase with Substrate Amppnp


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 Amppnp within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg511 b:52.0 occ:1.00 O A:HOH740 2.2 56.8 1.0 HZ3 A:LYS293 2.7 60.6 1.0 HA A:ALA130 2.9 42.8 1.0 H A:ALA131 3.1 41.8 1.0 HZ2 A:LYS293 3.3 60.6 1.0 HG2 A:LYS293 3.3 41.1 1.0 NZ A:LYS293 3.4 50.5 1.0 HB1 A:ALA130 3.5 42.5 1.0 HZ1 A:LYS293 3.8 60.6 1.0 CA A:ALA130 3.8 35.7 1.0 HB2 A:ALA130 3.9 42.5 1.0 CB A:ALA130 3.9 35.4 1.0 N A:ALA131 3.9 34.8 1.0 O A:HOH668 4.2 41.5 1.0 CG A:LYS293 4.3 34.3 1.0 C A:ALA130 4.4 34.7 1.0 HB3 A:ALA131 4.5 45.4 1.0 HG3 A:LYS293 4.6 41.1 1.0 CE A:LYS293 4.6 45.3 1.0 HA A:LYS293 4.7 48.8 1.0 O A:ARG129 4.7 40.1 1.0 HB2 A:ALA131 4.7 45.4 1.0 HD3 A:LYS293 4.7 51.9 1.0 CD A:LYS293 4.8 43.3 1.0 HB3 A:ALA130 4.8 42.5 1.0 N A:ALA130 4.9 35.8 1.0 CB A:ALA131 4.9 37.9 1.0 HE2 A:LYS293 5.0 54.4 1.0

Magnesium binding site 7 out of 38 in the Structure of the Bacterial Pathogens Atpase with Substrate Amppnp


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 Amppnp within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg512 b:48.0 occ:1.00 SE A:MSE171 2.0 28.8 1.0 HB3 A:PRO340 2.2 45.5 1.0 HD3 A:PRO340 2.3 47.6 1.0 HN61 A:ANP505 2.6 59.9 0.7 HG3 A:PRO340 2.7 51.4 1.0 CB A:PRO340 2.9 38.0 1.0 HE1 A:MSE171 2.9 42.5 1.0 CD A:PRO340 2.9 39.6 1.0 CG A:PRO340 3.0 42.8 1.0 CE A:MSE171 3.1 35.4 1.0 HN62 A:ANP505 3.1 59.9 0.7 N6 A:ANP505 3.2 49.9 0.7 N A:PRO340 3.5 41.6 1.0 HA A:PRO340 3.6 47.5 1.0 CA A:PRO340 3.6 39.6 1.0 O A:GLN410 3.7 40.7 1.0 HE3 A:MSE171 3.7 42.5 1.0 HB2 A:PRO340 3.7 45.5 1.0 HE2 A:MSE171 3.7 42.5 1.0 CG A:MSE171 3.8 30.0 1.0 HD2 A:PRO340 3.8 47.6 1.0 HA A:LEU168 3.9 41.8 1.0 HG2 A:PRO340 4.0 51.4 1.0 HG3 A:MSE171 4.0 36.0 1.0 HA A:TYR412 4.1 37.1 1.0 HD13 A:LEU168 4.1 43.8 1.0 HG2 A:MSE171 4.3 36.0 1.0 C A:PHE339 4.3 47.0 1.0 HB2 A:MSE171 4.4 40.0 1.0 HB3 A:GLN410 4.4 35.1 1.0 HB3 A:PHE339 4.4 64.6 1.0 HB3 A:PHE167 4.4 55.2 1.0 HD13 A:ILE140 4.5 43.9 1.0 HD12 A:LEU168 4.5 43.8 1.0 C6 A:ANP505 4.5 57.0 0.7 CB A:MSE171 4.5 33.3 1.0 HB3 A:TYR412 4.5 48.8 1.0 HB3 A:MSE171 4.6 40.0 1.0 CA A:LEU168 4.7 34.9 1.0 HB2 A:LEU168 4.8 34.8 1.0 O A:PHE339 4.8 38.9 1.0 CD1 A:LEU168 4.8 36.5 1.0 HG23 A:ILE140 4.8 27.9 1.0 CA A:TYR412 4.8 30.9 1.0 C A:GLN410 4.9 46.3 1.0 N A:LEU168 4.9 30.4 1.0 HG21 A:ILE140 5.0 27.9 1.0 HG2 A:GLN410 5.0 40.0 1.0 HB2 A:TYR412 5.0 48.8 1.0

Magnesium binding site 8 out of 38 in the Structure of the Bacterial Pathogens Atpase with Substrate Amppnp


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 Amppnp within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg513 b:53.6 occ:1.00 O A:HOH750 2.1 68.8 1.0 H A:TYR418 2.3 50.4 1.0 HB A:THR417 2.9 49.7 1.0 HD13 A:LEU137 3.0 40.9 1.0 N A:TYR418 3.2 42.0 1.0 HA A:THR417 3.3 49.4 1.0 HB3 A:TYR418 3.4 49.5 1.0 HB2 A:TYR418 3.5 49.5 1.0 OE1 A:GLU419 3.5 56.5 1.0 CB A:THR417 3.7 41.4 1.0 CD1 A:LEU137 3.7 34.1 1.0 HD12 A:LEU137 3.7 40.9 1.0 CB A:TYR418 3.8 41.2 1.0 CA A:THR417 3.8 41.2 1.0 HD11 A:LEU137 3.9 40.9 1.0 HG22 A:THR417 4.0 52.3 1.0 C A:THR417 4.0 40.3 1.0 CA A:TYR418 4.1 42.6 1.0 H A:GLU419 4.2 40.8 1.0 CG2 A:THR417 4.3 43.6 1.0 CD A:GLU419 4.4 60.0 1.0 OE2 A:GLU419 4.4 56.8 1.0 HG21 A:THR417 4.7 52.3 1.0 HA A:TYR418 4.7 51.1 1.0 OG1 A:THR417 4.8 38.8 1.0 HB3 A:LEU137 4.9 41.2 1.0 N A:GLU419 4.9 34.0 1.0

Magnesium binding site 9 out of 38 in the Structure of the Bacterial Pathogens Atpase with Substrate Amppnp


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 Amppnp within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg514 b:60.5 occ:1.00 O A:GLY100 2.3 50.6 1.0 O A:HOH639 2.6 32.5 1.0 HB2 A:GLN86 2.7 41.0 1.0 HG11 A:VAL96 2.8 42.6 1.0 HA2 A:GLY100 2.9 55.1 1.0 HG13 A:VAL96 3.0 42.6 1.0 O A:HOH701 3.1 36.7 1.0 C A:GLY100 3.1 47.4 1.0 CG1 A:VAL96 3.3 35.5 1.0 HD21 A:LEU91 3.4 46.7 1.0 CA A:GLY100 3.4 45.9 1.0 OE1 A:GLN86 3.4 49.8 1.0 HA3 A:GLY100 3.5 55.1 1.0 CB A:GLN86 3.6 34.1 1.0 H A:GLN86 3.7 45.0 1.0 HG12 A:VAL96 3.8 42.6 1.0 HG3 A:GLN86 3.8 49.9 1.0 HG1 A:THR85 3.8 42.4 1.0 HD22 A:LEU91 3.9 46.7 1.0 HD11 A:LEU91 4.0 48.5 1.0 CD A:GLN86 4.0 48.1 1.0 CG A:GLN86 4.0 41.6 1.0 CD2 A:LEU91 4.1 38.9 1.0 HB3 A:GLN86 4.1 41.0 1.0 HG21 A:VAL96 4.1 52.6 1.0 HG22 A:VAL96 4.3 52.6 1.0 N A:GLU101 4.3 45.9 1.0 OG1 A:THR85 4.4 35.3 1.0 N A:GLN86 4.4 37.5 1.0 HD13 A:LEU91 4.5 48.5 1.0 HA A:GLU101 4.5 58.3 1.0 CG2 A:VAL96 4.5 43.8 1.0 CB A:VAL96 4.5 32.4 1.0 CA A:GLN86 4.6 39.5 1.0 CD1 A:LEU91 4.6 40.4 1.0 HG22 A:VAL102 4.7 46.0 1.0 HD23 A:LEU91 4.7 46.7 1.0 N A:GLY100 4.8 39.5 1.0 O A:GLN86 4.8 36.2 1.0 CA A:GLU101 4.9 48.5 1.0 HG23 A:VAL102 4.9 46.0 1.0 H A:GLY100 5.0 47.5 1.0 CG A:LEU91 5.0 42.4 1.0 HG2 A:GLN86 5.0 49.9 1.0

Magnesium binding site 10 out of 38 in the Structure of the Bacterial Pathogens Atpase with Substrate Amppnp


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 Amppnp within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg515 b:48.5 occ:1.00 HE A:ARG368 2.0 53.5 1.0 NE A:ARG368 2.8 44.6 1.0 HB3 A:LEU146 3.0 39.4 1.0 HD3 A:ARG368 3.1 47.5 1.0 O A:LEU146 3.2 34.2 1.0 HD21 A:LEU147 3.2 35.3 1.0 HH21 A:ARG368 3.3 44.3 1.0 HB2 A:SER344 3.3 49.6 1.0 HD23 A:LEU147 3.3 35.3 1.0 CD A:ARG368 3.5 39.5 1.0 O A:SER344 3.7 36.1 1.0 CD2 A:LEU147 3.7 29.4 1.0 CZ A:ARG368 3.7 49.7 1.0 NH2 A:ARG368 3.8 36.9 1.0 HD13 A:LEU146 3.8 46.2 1.0 HG A:LEU147 3.9 31.2 1.0 CB A:LEU146 3.9 32.8 1.0 HG2 A:ARG368 4.0 49.7 1.0 C A:LEU146 4.1 28.8 1.0 HB2 A:LEU146 4.2 39.4 1.0 CB A:SER344 4.2 41.3 1.0 HD2 A:ARG368 4.3 47.5 1.0 CG A:ARG368 4.3 41.4 1.0 O A:HOH694 4.4 28.6 1.0 C A:SER344 4.4 41.1 1.0 CG A:LEU147 4.4 26.0 1.0 HA A:SER344 4.5 51.5 1.0 O A:SER347 4.5 38.9 1.0 HD22 A:LEU147 4.5 35.3 1.0 CA A:LEU146 4.5 30.3 1.0 HA A:LEU146 4.6 36.4 1.0 CD1 A:LEU146 4.6 38.5 1.0 HH22 A:ARG368 4.6 44.3 1.0 HD12 A:LEU146 4.6 46.2 1.0 CA A:SER344 4.7 42.9 1.0 HG3 A:ARG368 4.7 49.7 1.0 HD22 A:LEU146 4.7 50.4 1.0 HA A:ILE348 4.7 38.8 1.0 OG A:SER344 4.8 47.9 1.0 CG A:LEU146 4.8 41.7 1.0 HB3 A:SER344 4.8 49.6 1.0 HG A:SER344 4.9 57.5 1.0 NH1 A:ARG368 5.0 44.6 1.0 O A:HOH745 5.0 40.1 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 From Shigella Flexneri Front Microbiol V. 9 1468 2018.
ISSN: ESSN 1664-302X
DOI: 10.3389/FMICB.2018.01468