Magnesium in PDB 6n6n: Ftsy-Ng High-Resolution

Protein crystallography data

The structure of Ftsy-Ng High-Resolution, PDB code: 6n6n was solved by S.F.Ataide, C.Faoro, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 36.17 / 1.88
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 35.420, 76.883, 106.935, 90.00, 92.54, 90.00
R / Rfree (%) 19.5 / 24.3

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Ftsy-Ng High-Resolution (pdb code 6n6n). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 5 binding sites of Magnesium where determined in the Ftsy-Ng High-Resolution, PDB code: 6n6n:
Jump to Magnesium binding site number: 1; 2; 3; 4; 5;

Magnesium binding site 1 out of 5 in 6n6n

Go back to Magnesium Binding Sites List in 6n6n
Magnesium binding site 1 out of 5 in the Ftsy-Ng High-Resolution


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Ftsy-Ng High-Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg502

b:55.4
occ:1.00
HG1 A:THR307 1.6 36.2 1.0
O1G A:GCP501 1.8 68.7 1.0
O A:HOH746 1.9 65.2 1.0
O A:HOH622 2.2 30.0 1.0
OG1 A:THR307 2.3 30.2 1.0
O A:HOH642 2.7 46.9 1.0
O1B A:GCP501 2.7 38.0 1.0
PG A:GCP501 3.2 84.2 1.0
HB A:THR307 3.3 42.7 1.0
CB A:THR307 3.3 35.6 1.0
HG21 A:THR307 3.4 40.4 1.0
HH21 A:ARG333 3.4 93.4 1.0
O A:HOH624 3.6 29.6 1.0
HH22 A:ARG333 3.7 93.4 1.0
O A:HOH638 3.8 28.5 1.0
CG2 A:THR307 3.9 33.7 1.0
PB A:GCP501 3.9 54.9 1.0
NH2 A:ARG333 3.9 77.8 1.0
C3B A:GCP501 3.9 65.8 1.0
H3B1 A:GCP501 4.0 79.0 1.0
O3G A:GCP501 4.0 91.7 1.0
HB3 A:ALA336 4.0 37.8 1.0
HB1 A:ALA336 4.2 37.8 1.0
HG23 A:THR307 4.2 40.4 1.0
O2G A:GCP501 4.3 56.8 1.0
HA A:ALA336 4.3 34.9 1.0
HD22 A:ASN302 4.3 58.8 1.0
H A:THR307 4.4 30.6 1.0
CB A:ALA336 4.5 31.4 1.0
O2A A:GCP501 4.5 56.4 1.0
OE1 A:GLN339 4.6 55.6 1.0
CA A:THR307 4.7 30.5 1.0
HG22 A:THR307 4.7 40.4 1.0
O2B A:GCP501 4.7 54.5 1.0
HD21 A:ASN302 4.9 58.8 1.0
H3B2 A:GCP501 4.9 79.0 1.0
N A:THR307 4.9 25.5 1.0
HA A:THR307 4.9 36.6 1.0
ND2 A:ASN302 4.9 49.0 1.0
CA A:ALA336 4.9 29.1 1.0
HE22 A:GLN339 5.0 69.8 1.0

Magnesium binding site 2 out of 5 in 6n6n

Go back to Magnesium Binding Sites List in 6n6n
Magnesium binding site 2 out of 5 in the Ftsy-Ng High-Resolution


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Ftsy-Ng High-Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg503

b:83.5
occ:1.00
HB3 A:GLU230 1.8 44.3 1.0
O A:HOH693 1.9 34.8 1.0
HA A:GLU230 2.0 44.6 1.0
O A:GLU230 2.0 27.3 1.0
CA A:GLU230 2.2 37.2 1.0
C A:GLU230 2.3 29.5 1.0
CB A:GLU230 2.4 36.9 1.0
HB3 A:GLU233 3.0 33.4 1.0
HD11 A:LEU217 3.0 45.3 1.0
HB2 A:GLU230 3.1 44.3 1.0
HG2 A:GLU230 3.2 57.0 1.0
CG A:GLU230 3.4 47.5 1.0
N A:LEU231 3.5 25.3 1.0
OE1 A:GLU233 3.6 25.0 1.0
N A:GLU230 3.7 22.4 1.0
H A:GLN234 3.7 33.9 1.0
O A:HOH731 3.7 34.8 1.0
HB2 A:GLN234 3.8 28.3 1.0
HD13 A:LEU217 3.8 45.3 1.0
CD1 A:LEU217 3.9 37.8 1.0
HD21 A:LEU217 3.9 47.0 1.0
CB A:GLU233 4.0 27.8 1.0
OE1 A:GLU230 4.0 47.4 1.0
H A:LEU231 4.0 30.4 1.0
HG3 A:GLU230 4.1 57.0 1.0
HA A:LEU231 4.1 29.2 1.0
H A:GLU230 4.2 26.8 1.0
CD A:GLU230 4.2 49.2 1.0
O A:GLU229 4.3 29.8 1.0
H A:GLU233 4.3 38.0 1.0
HB2 A:GLU233 4.3 33.4 1.0
O A:HOH758 4.3 50.0 1.0
N A:GLN234 4.4 28.3 1.0
CA A:LEU231 4.4 24.4 1.0
C A:GLU229 4.4 22.1 1.0
HD12 A:LEU217 4.4 45.3 1.0
CD A:GLU233 4.5 40.2 1.0
HD22 A:LEU217 4.6 47.0 1.0
CD2 A:LEU217 4.6 39.2 1.0
CG A:GLU233 4.7 28.8 1.0
CB A:GLN234 4.7 23.6 1.0
HG2 A:GLU233 4.7 34.6 1.0
N A:GLU233 4.8 31.6 1.0
CG A:LEU217 4.8 39.8 1.0
HB3 A:GLN234 4.8 28.3 1.0
CA A:GLU233 4.8 36.5 1.0
C A:LEU231 4.9 26.1 1.0

Magnesium binding site 3 out of 5 in 6n6n

Go back to Magnesium Binding Sites List in 6n6n
Magnesium binding site 3 out of 5 in the Ftsy-Ng High-Resolution


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Ftsy-Ng High-Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg504

b:60.0
occ:1.00
OE2 A:GLU229 2.1 58.4 1.0
HB2 A:GLU229 2.7 35.4 1.0
HB3 A:GLU229 2.7 35.4 1.0
CB A:GLU229 3.1 29.5 1.0
CD A:GLU229 3.2 48.8 1.0
HA A:ASP226 3.7 42.5 1.0
CG A:GLU229 3.7 38.2 1.0
OE1 A:GLU229 4.3 50.9 1.0
OD1 A:ASP226 4.3 52.1 1.0
HG3 A:GLU229 4.3 45.8 1.0
HG2 A:GLU229 4.4 45.8 1.0
O A:ASP226 4.4 28.6 1.0
CA A:GLU229 4.4 32.7 1.0
CA A:ASP226 4.6 35.4 1.0
C A:GLU229 4.6 22.1 1.0
H A:GLU230 4.7 26.8 1.0
HG3 A:GLU230 4.8 57.0 1.0
N A:GLU230 4.8 22.4 1.0
HB3 A:ASP226 4.8 43.2 1.0
CG A:ASP226 4.9 49.7 1.0
C A:ASP226 5.0 31.0 1.0

Magnesium binding site 4 out of 5 in 6n6n

Go back to Magnesium Binding Sites List in 6n6n
Magnesium binding site 4 out of 5 in the Ftsy-Ng High-Resolution


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Ftsy-Ng High-Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg503

b:28.2
occ:1.00
O2B B:GCP501 2.0 25.4 1.0
O B:HOH746 2.0 36.8 1.0
O2G B:GCP501 2.1 27.0 1.0
OG1 B:THR307 2.1 28.0 1.0
O B:HOH655 2.1 25.8 1.0
O B:HOH687 2.2 37.1 1.0
HG1 B:THR307 2.7 33.6 1.0
HB B:THR307 2.9 29.9 1.0
CB B:THR307 3.0 24.9 1.0
HH22 B:ARG333 3.1 31.5 1.0
PG B:GCP501 3.3 32.5 1.0
PB B:GCP501 3.3 34.0 1.0
H B:THR307 3.5 27.4 1.0
C3B B:GCP501 3.6 40.7 1.0
H3B2 B:GCP501 3.6 48.9 1.0
HG21 B:THR307 3.7 35.5 1.0
HH21 B:ARG333 3.7 31.5 1.0
NH2 B:ARG333 3.8 26.2 1.0
O3G B:GCP501 3.9 34.6 1.0
CG2 B:THR307 4.0 29.6 1.0
N B:THR307 4.1 22.9 1.0
O1A B:GCP501 4.1 39.4 1.0
CA B:THR307 4.2 25.0 1.0
O1B B:GCP501 4.2 36.6 1.0
O B:HOH650 4.3 25.4 1.0
O B:HOH645 4.3 22.6 1.0
HG23 B:THR307 4.4 35.5 1.0
O B:HOH639 4.4 24.0 1.0
O3A B:GCP501 4.5 33.0 1.0
O1G B:GCP501 4.5 39.8 1.0
H3B1 B:GCP501 4.5 48.9 1.0
HA B:THR307 4.5 30.1 1.0
O2A B:GCP501 4.7 28.5 1.0
PA B:GCP501 4.7 43.8 1.0
HB2 B:ALA336 4.7 28.4 1.0
HG22 B:THR307 4.7 35.5 1.0
HB3 B:LYS306 4.8 27.9 1.0
CZ B:ARG333 5.0 21.8 1.0

Magnesium binding site 5 out of 5 in 6n6n

Go back to Magnesium Binding Sites List in 6n6n
Magnesium binding site 5 out of 5 in the Ftsy-Ng High-Resolution


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 5 of Ftsy-Ng High-Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg504

b:35.1
occ:1.00
O B:HOH606 1.9 49.7 1.0
OD1 B:ASP283 2.2 26.1 1.0
O B:HOH722 2.4 25.9 1.0
O B:PHE483 2.5 17.5 1.0
HG3 B:PRO285 2.8 36.1 1.0
O A:HOH757 2.9 25.9 1.0
HD3 B:PRO285 3.1 30.4 1.0
HA B:LYS484 3.2 24.0 1.0
CG B:ASP283 3.3 22.1 1.0
HA B:ASP283 3.4 24.8 1.0
CG B:PRO285 3.6 30.1 1.0
CD B:PRO285 3.6 25.3 1.0
O B:HOH728 3.6 23.5 1.0
C B:ASP283 3.6 27.6 1.0
C B:PHE483 3.6 14.9 1.0
N B:GLU284 3.6 20.2 1.0
N B:PRO285 3.7 22.1 1.0
H B:GLU284 3.8 24.2 1.0
HA B:PRO285 3.9 21.2 1.0
CA B:ASP283 3.9 20.7 1.0
HD2 B:PHE483 3.9 21.6 1.0
C B:GLU284 3.9 21.9 1.0
O B:ASP283 4.0 31.7 1.0
H B:ALA485 4.0 22.9 1.0
HG2 B:LYS484 4.1 28.3 1.0
OD2 B:ASP283 4.1 26.7 1.0
CA B:LYS484 4.1 20.0 1.0
HA B:GLU284 4.1 24.4 1.0
CA B:GLU284 4.2 20.3 1.0
CB B:ASP283 4.2 19.4 1.0
CA B:PRO285 4.2 17.7 1.0
HG2 B:PRO285 4.3 36.1 1.0
HA2 A:GLY195 4.3 35.8 1.0
N B:LYS484 4.3 14.4 1.0
HB3 B:PHE483 4.4 26.8 1.0
CB B:PRO285 4.4 21.4 1.0
O B:HOH648 4.4 22.4 1.0
HB3 B:PRO285 4.5 25.7 1.0
HD2 B:PRO285 4.5 30.4 1.0
CD2 B:PHE483 4.5 18.0 1.0
O B:GLU284 4.5 22.5 1.0
N A:GLY195 4.6 25.7 1.0
HB3 B:ASP283 4.7 23.2 1.0
N B:ALA485 4.7 19.1 1.0
CA B:PHE483 4.8 19.5 1.0
CG B:LYS484 4.8 23.6 1.0
HB2 B:ASP283 4.9 23.2 1.0
O B:ILE468 4.9 17.9 1.0
CB B:PHE483 4.9 22.3 1.0
O B:HOH837 4.9 34.3 1.0
HG3 B:LYS484 5.0 28.3 1.0
CA A:GLY195 5.0 29.8 1.0
C B:LYS484 5.0 17.8 1.0
CB B:LYS484 5.0 21.2 1.0

Reference:

C.Faoro, S.F.Ataide. Structural Insights Into the G-Loop Dynamics of E. Coli Ftsy Ng Domain. J.Struct.Biol. V. 208 2019.
ISSN: ESSN 1095-8657
PubMed: 31520694
DOI: 10.1016/J.JSB.2019.09.004
Page generated: Mon Dec 14 23:39:38 2020

Last articles

Zn in 8WB0
Zn in 8WAX
Zn in 8WAU
Zn in 8WAZ
Zn in 8WAY
Zn in 8WAV
Zn in 8WAW
Zn in 8WAT
Zn in 8W7M
Zn in 8WD3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy