Magnesium in PDB 7njl: Mycobacterium Smegmatis Atp Synthase State 1B

Enzymatic activity of Mycobacterium Smegmatis Atp Synthase State 1B

All present enzymatic activity of Mycobacterium Smegmatis Atp Synthase State 1B:
7.1.2.2;

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Mycobacterium Smegmatis Atp Synthase State 1B (pdb code 7njl). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 5 binding sites of Magnesium where determined in the Mycobacterium Smegmatis Atp Synthase State 1B, PDB code: 7njl:
Jump to Magnesium binding site number: 1; 2; 3; 4; 5;

Magnesium binding site 1 out of 5 in 7njl

Go back to Magnesium Binding Sites List in 7njl
Magnesium binding site 1 out of 5 in the Mycobacterium Smegmatis Atp Synthase State 1B


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Mycobacterium Smegmatis Atp Synthase State 1B within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg601

b:38.8
occ:1.00
O2G A:ATP600 2.2 43.0 1.0
O A:HOH703 2.2 42.9 1.0
O2B A:ATP600 2.2 43.0 1.0
O A:HOH702 2.2 41.1 1.0
O A:HOH701 2.2 45.8 1.0
OG1 A:THR179 2.2 41.2 1.0
HB A:THR179 3.0 41.2 1.0
CB A:THR179 3.1 41.2 1.0
H A:THR179 3.3 41.2 1.0
PB A:ATP600 3.4 43.0 1.0
PG A:ATP600 3.4 43.0 1.0
O3B A:ATP600 3.4 43.0 1.0
OD2 A:ASP272 3.8 40.5 1.0
HG21 A:THR179 4.0 41.2 1.0
N A:THR179 4.0 41.2 1.0
OD1 A:ASP272 4.0 40.5 1.0
O1A A:ATP600 4.1 43.0 1.0
CG2 A:THR179 4.2 41.2 1.0
CA A:THR179 4.2 41.2 1.0
O3A A:ATP600 4.3 43.0 1.0
HB2 A:LYS178 4.3 41.5 1.0
O3G A:ATP600 4.3 43.0 1.0
CG A:ASP272 4.4 40.5 1.0
O1G A:ATP600 4.4 43.0 1.0
O1B A:ATP600 4.5 43.0 1.0
HE2 A:LYS178 4.5 41.5 1.0
PA A:ATP600 4.5 43.0 1.0
HA A:THR179 4.6 41.2 1.0
O2A A:ATP600 4.7 43.0 1.0
HG23 A:THR179 4.7 41.2 1.0
HG22 A:THR179 4.8 41.2 1.0
HG21 A:ILE329 5.0 40.1 1.0

Magnesium binding site 2 out of 5 in 7njl

Go back to Magnesium Binding Sites List in 7njl
Magnesium binding site 2 out of 5 in the Mycobacterium Smegmatis Atp Synthase State 1B


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Mycobacterium Smegmatis Atp Synthase State 1B within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg601

b:45.7
occ:1.00
OG1 B:THR179 2.2 44.7 1.0
O2G B:ATP600 2.2 47.6 1.0
O B:HOH702 2.2 45.6 1.0
O B:HOH703 2.2 43.5 1.0
O B:HOH701 2.2 43.5 1.0
O2B B:ATP600 2.2 47.6 1.0
HB B:THR179 2.9 44.7 1.0
CB B:THR179 3.1 44.7 1.0
PB B:ATP600 3.4 47.6 1.0
H B:THR179 3.4 44.7 1.0
PG B:ATP600 3.4 47.6 1.0
O3B B:ATP600 3.4 47.6 1.0
OD2 B:ASP272 3.6 42.0 1.0
HE22 B:GLN211 3.7 43.0 1.0
HG21 B:THR179 3.9 44.7 1.0
HE21 B:GLN211 4.0 43.0 1.0
NE2 B:GLN211 4.0 43.0 1.0
OD1 B:ASP272 4.0 42.0 1.0
N B:THR179 4.0 44.7 1.0
CG2 B:THR179 4.1 44.7 1.0
CA B:THR179 4.1 44.7 1.0
CG B:ASP272 4.3 42.0 1.0
O3G B:ATP600 4.3 47.6 1.0
O3A B:ATP600 4.4 47.6 1.0
O1B B:ATP600 4.4 47.6 1.0
O1A B:ATP600 4.4 47.6 1.0
O1G B:ATP600 4.4 47.6 1.0
HB2 B:LYS178 4.4 45.0 1.0
HA B:THR179 4.5 44.7 1.0
HE2 B:LYS178 4.6 45.0 1.0
HG22 B:THR179 4.7 44.7 1.0
HG23 B:THR179 4.7 44.7 1.0
PA B:ATP600 4.8 47.6 1.0
O2A B:ATP600 4.9 47.6 1.0
CD B:GLN211 4.9 43.0 1.0
HH B:TYR206 5.0 40.8 1.0

Magnesium binding site 3 out of 5 in 7njl

Go back to Magnesium Binding Sites List in 7njl
Magnesium binding site 3 out of 5 in the Mycobacterium Smegmatis Atp Synthase State 1B


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Mycobacterium Smegmatis Atp Synthase State 1B within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg601

b:39.9
occ:1.00
OG1 C:THR179 2.2 42.5 1.0
O C:HOH703 2.2 42.2 1.0
O C:HOH701 2.2 44.5 1.0
O2G C:ATP600 2.2 42.8 1.0
O C:HOH702 2.2 40.9 1.0
O2B C:ATP600 2.2 42.8 1.0
HB C:THR179 3.0 42.5 1.0
CB C:THR179 3.1 42.5 1.0
O3B C:ATP600 3.3 42.8 1.0
PB C:ATP600 3.3 42.8 1.0
H C:THR179 3.4 42.5 1.0
PG C:ATP600 3.4 42.8 1.0
OD2 C:ASP272 3.7 42.7 1.0
OD1 C:ASP272 4.0 42.7 1.0
HG21 C:THR179 4.0 42.5 1.0
N C:THR179 4.0 42.5 1.0
CA C:THR179 4.1 42.5 1.0
CG2 C:THR179 4.2 42.5 1.0
O3G C:ATP600 4.2 42.8 1.0
HE21 C:GLN211 4.2 43.9 1.0
CG C:ASP272 4.2 42.7 1.0
O3A C:ATP600 4.3 42.8 1.0
HE22 C:GLN211 4.3 43.9 1.0
HB2 C:LYS178 4.3 42.3 1.0
O1A C:ATP600 4.3 42.8 1.0
HE2 C:LYS178 4.3 42.3 1.0
O1B C:ATP600 4.4 42.8 1.0
O1G C:ATP600 4.5 42.8 1.0
HA C:THR179 4.5 42.5 1.0
NE2 C:GLN211 4.5 43.9 1.0
PA C:ATP600 4.6 42.8 1.0
O2A C:ATP600 4.7 42.8 1.0
HG23 C:THR179 4.8 42.5 1.0
HG22 C:THR179 4.8 42.5 1.0
HD13 C:ILE329 4.9 41.5 1.0
HG21 C:ILE329 5.0 41.5 1.0

Magnesium binding site 4 out of 5 in 7njl

Go back to Magnesium Binding Sites List in 7njl
Magnesium binding site 4 out of 5 in the Mycobacterium Smegmatis Atp Synthase State 1B


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Mycobacterium Smegmatis Atp Synthase State 1B within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mg601

b:44.3
occ:1.00
OG1 D:THR167 2.2 42.5 1.0
O D:HOH701 2.2 42.6 1.0
O D:HOH704 2.2 42.7 1.0
O2B D:ADP600 2.2 43.3 1.0
O D:HOH702 2.2 43.9 1.0
O D:HOH703 2.2 44.3 1.0
HB D:THR167 3.2 42.5 1.0
HH12 D:ARG193 3.2 43.3 1.0
CB D:THR167 3.2 42.5 1.0
PB D:ADP600 3.4 43.3 1.0
H D:THR167 3.6 42.5 1.0
HH11 D:ARG193 3.7 43.3 1.0
NH1 D:ARG193 3.7 43.3 1.0
O3B D:ADP600 3.7 43.3 1.0
O3A D:ADP600 3.8 43.3 1.0
OE2 D:GLU196 3.8 44.5 1.0
HH11 C:ARG376 4.0 42.8 1.0
HH12 C:ARG376 4.0 42.8 1.0
OE1 D:GLU196 4.0 44.5 1.0
HG21 D:THR167 4.0 42.5 1.0
OE1 D:GLU192 4.1 43.9 1.0
N D:THR167 4.1 42.5 1.0
HB2 D:LYS166 4.2 41.1 1.0
OD2 D:ASP254 4.2 42.2 1.0
CA D:THR167 4.2 42.5 1.0
O2A D:ADP600 4.2 43.3 1.0
CG2 D:THR167 4.3 42.5 1.0
CD D:GLU196 4.3 44.5 1.0
NH1 C:ARG376 4.3 42.8 1.0
HE2 D:LYS166 4.4 41.1 1.0
PA D:ADP600 4.4 43.3 1.0
CD D:GLU192 4.4 43.9 1.0
OD1 D:ASP254 4.4 42.2 1.0
O1A D:ADP600 4.4 43.3 1.0
HA D:THR167 4.5 42.5 1.0
HG3 D:GLU192 4.5 43.9 1.0
OE2 D:GLU192 4.6 43.9 1.0
O1B D:ADP600 4.7 43.3 1.0
CG D:ASP254 4.7 42.2 1.0
HD22 D:ASN255 4.8 41.5 1.0
HG23 D:THR167 4.8 42.5 1.0
HZ1 D:LYS166 4.9 41.1 1.0
HZ3 D:LYS166 4.9 41.1 1.0
HG22 D:THR167 4.9 42.5 1.0
CZ D:ARG193 4.9 43.3 1.0
CG D:GLU192 5.0 43.9 1.0

Magnesium binding site 5 out of 5 in 7njl

Go back to Magnesium Binding Sites List in 7njl
Magnesium binding site 5 out of 5 in the Mycobacterium Smegmatis Atp Synthase State 1B


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 5 of Mycobacterium Smegmatis Atp Synthase State 1B within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Mg601

b:42.4
occ:1.00
O2G F:ATP600 2.2 44.6 1.0
O2B F:ATP600 2.2 44.6 1.0
OG1 F:THR167 2.2 42.6 1.0
O F:HOH701 2.2 44.1 1.0
O F:HOH702 2.2 43.0 1.0
O F:HOH703 2.2 44.4 1.0
HB F:THR167 3.0 42.6 1.0
HH12 F:ARG193 3.0 42.7 1.0
CB F:THR167 3.1 42.6 1.0
H F:THR167 3.4 42.6 1.0
PB F:ATP600 3.4 44.6 1.0
PG F:ATP600 3.4 44.6 1.0
O3B F:ATP600 3.4 44.6 1.0
NH1 F:ARG193 3.8 42.7 1.0
OE2 F:GLU196 3.8 43.7 1.0
HH12 B:ARG376 3.8 45.8 1.0
HH11 F:ARG193 3.9 42.7 1.0
N F:THR167 4.0 42.6 1.0
HG21 F:THR167 4.0 42.6 1.0
OE1 F:GLU196 4.0 43.7 1.0
OE1 F:GLU192 4.1 43.8 1.0
CA F:THR167 4.1 42.6 1.0
OD2 F:ASP254 4.1 42.5 1.0
O2A F:ATP600 4.1 44.6 1.0
HB2 F:LYS166 4.1 41.9 1.0
CG2 F:THR167 4.2 42.6 1.0
O3A F:ATP600 4.3 44.6 1.0
CD F:GLU196 4.3 43.7 1.0
O3G F:ATP600 4.4 44.6 1.0
HE2 F:LYS166 4.4 41.9 1.0
O1G F:ATP600 4.4 44.6 1.0
HA F:THR167 4.4 42.6 1.0
O1B F:ATP600 4.5 44.6 1.0
NH1 B:ARG376 4.6 45.8 1.0
PA F:ATP600 4.6 44.6 1.0
HZ1 F:LYS166 4.6 41.9 1.0
HZ3 F:LYS166 4.6 41.9 1.0
O1A F:ATP600 4.7 44.6 1.0
CD F:GLU192 4.7 43.8 1.0
OD1 F:ASP254 4.7 42.5 1.0
HH11 B:ARG376 4.7 45.8 1.0
HH22 F:ARG193 4.7 42.7 1.0
HG23 F:THR167 4.8 42.6 1.0
HG22 F:THR167 4.8 42.6 1.0
CG F:ASP254 4.9 42.5 1.0
HG3 F:GLU192 4.9 43.8 1.0
CZ F:ARG193 4.9 42.7 1.0
NZ F:LYS166 5.0 41.9 1.0

Reference:

J.Petri, M.G.Montgomery, T.J.Spikes, G.M.Cook, J.E.Walker. Structure of the Atp Synthase From Mycobacterium Smegmatis To Be Published.
Page generated: Fri Nov 5 15:25:09 2021

Last articles

Zn in 7VD8
Zn in 7V1R
Zn in 7V1Q
Zn in 7VPF
Zn in 7T85
Zn in 7T5F
Zn in 7NF9
Zn in 7M4M
Zn in 7M4O
Zn in 7M4N
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy