Atomistry » Magnesium » PDB 3u8u-3umo » 3umm
Atomistry »
  Magnesium »
    PDB 3u8u-3umo »
      3umm »

Magnesium in PDB 3umm: Formylglycinamide Ribonucleotide Amidotransferase From Salmonella Typhimurium: Role of the Atp Complexation and Glutaminase Domain in Catalytic Coupling

Enzymatic activity of Formylglycinamide Ribonucleotide Amidotransferase From Salmonella Typhimurium: Role of the Atp Complexation and Glutaminase Domain in Catalytic Coupling

All present enzymatic activity of Formylglycinamide Ribonucleotide Amidotransferase From Salmonella Typhimurium: Role of the Atp Complexation and Glutaminase Domain in Catalytic Coupling:
6.3.5.3;

Protein crystallography data

The structure of Formylglycinamide Ribonucleotide Amidotransferase From Salmonella Typhimurium: Role of the Atp Complexation and Glutaminase Domain in Catalytic Coupling, PDB code: 3umm was solved by R.Anand, M.Morar, A.S.Tanwar, S.Panjikar, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.98 / 3.20
Space group P 65
Cell size a, b, c (Å), α, β, γ (°) 148.680, 148.680, 142.050, 90.00, 90.00, 120.00
R / Rfree (%) 19.6 / 27.6

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Formylglycinamide Ribonucleotide Amidotransferase From Salmonella Typhimurium: Role of the Atp Complexation and Glutaminase Domain in Catalytic Coupling (pdb code 3umm). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 3 binding sites of Magnesium where determined in the Formylglycinamide Ribonucleotide Amidotransferase From Salmonella Typhimurium: Role of the Atp Complexation and Glutaminase Domain in Catalytic Coupling, PDB code: 3umm:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in 3umm

Go back to Magnesium Binding Sites List in 3umm
Magnesium binding site 1 out of 3 in the Formylglycinamide Ribonucleotide Amidotransferase From Salmonella Typhimurium: Role of the Atp Complexation and Glutaminase Domain in Catalytic Coupling


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Formylglycinamide Ribonucleotide Amidotransferase From Salmonella Typhimurium: Role of the Atp Complexation and Glutaminase Domain in Catalytic Coupling within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg2006

b:30.2
occ:1.00
O3B A:ADP2005 2.2 30.3 0.5
OE2 A:GLU718 2.2 30.5 1.0
CD A:GLU718 3.2 30.5 1.0
O1A A:ADP2005 3.4 30.3 0.5
OE1 A:GLU718 3.6 30.5 1.0
PB A:ADP2005 3.7 30.3 0.5
OD2 A:ASP887 3.8 33.4 1.0
OE1 A:GLU699 4.2 36.9 1.0
O3A A:ADP2005 4.2 30.3 0.5
O A:GLU699 4.3 19.9 1.0
O2B A:ADP2005 4.3 30.3 0.5
PA A:ADP2005 4.4 30.3 0.5
O A:ILE697 4.5 19.3 1.0
CB A:TYR388 4.6 24.6 1.0
CG A:GLU718 4.6 30.5 1.0
O1B A:ADP2005 4.6 30.3 0.5
OG A:SER886 4.7 44.8 1.0
ND2 A:ASN722 4.8 35.0 1.0
CG A:ASP887 4.9 33.4 1.0
CB A:SER886 5.0 44.8 1.0

Magnesium binding site 2 out of 3 in 3umm

Go back to Magnesium Binding Sites List in 3umm
Magnesium binding site 2 out of 3 in the Formylglycinamide Ribonucleotide Amidotransferase From Salmonella Typhimurium: Role of the Atp Complexation and Glutaminase Domain in Catalytic Coupling


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Formylglycinamide Ribonucleotide Amidotransferase From Salmonella Typhimurium: Role of the Atp Complexation and Glutaminase Domain in Catalytic Coupling within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg2007

b:30.2
occ:1.00
O2A A:ADP2005 2.2 30.3 0.5
O2B A:ADP2005 2.6 30.3 0.5
PA A:ADP2005 3.4 30.3 0.5
OG A:SER886 3.6 44.8 1.0
PB A:ADP2005 3.7 30.3 0.5
O3A A:ADP2005 3.8 30.3 0.5
O1A A:ADP2005 4.0 30.3 0.5
OD2 A:ASP887 4.0 33.4 1.0
CB A:ASP887 4.2 33.4 1.0
O3B A:ADP2005 4.2 30.3 0.5
OE2 A:GLU896 4.2 21.3 1.0
O A:ASP887 4.2 33.5 1.0
OE1 A:GLU896 4.4 21.3 1.0
O A:THR645 4.6 18.1 1.0
O5' A:ADP2005 4.6 30.3 1.0
CG A:ASP887 4.6 33.4 1.0
N A:ASP887 4.6 33.5 1.0
CD A:GLU896 4.8 21.3 1.0
MG A:MG2008 4.8 30.2 1.0
CA A:ASP887 4.8 33.5 1.0
O A:VAL646 4.9 14.7 1.0
CB A:SER886 4.9 44.8 1.0
O1B A:ADP2005 5.0 30.3 0.5
C A:ASP887 5.0 33.5 1.0
C5' A:ADP2005 5.0 30.3 1.0

Magnesium binding site 3 out of 3 in 3umm

Go back to Magnesium Binding Sites List in 3umm
Magnesium binding site 3 out of 3 in the Formylglycinamide Ribonucleotide Amidotransferase From Salmonella Typhimurium: Role of the Atp Complexation and Glutaminase Domain in Catalytic Coupling


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Formylglycinamide Ribonucleotide Amidotransferase From Salmonella Typhimurium: Role of the Atp Complexation and Glutaminase Domain in Catalytic Coupling within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg2008

b:30.2
occ:1.00
O1B A:ADP2005 2.2 30.3 0.5
OD1 A:ASP884 2.2 29.8 1.0
O2B A:ADP2005 2.3 30.3 0.5
OD1 A:ASP679 2.4 26.5 1.0
OD1 A:ASN722 2.5 35.0 1.0
PB A:ADP2005 2.6 30.3 0.5
OD2 A:ASP884 2.9 29.8 1.0
CG A:ASP884 2.9 29.8 1.0
CG A:ASN722 3.5 35.0 1.0
O3B A:ADP2005 3.5 30.3 0.5
CG A:ASP679 3.5 26.5 1.0
ND2 A:ASN722 3.7 35.0 1.0
OG A:SER886 3.9 44.8 1.0
O3A A:ADP2005 3.9 30.3 0.5
O A:HOH1563 4.0 28.7 1.0
OD2 A:ASP679 4.3 26.5 1.0
CB A:ASP884 4.4 29.8 1.0
CB A:ASP679 4.5 26.5 1.0
NE2 A:HIS883 4.5 19.9 1.0
CD2 A:HIS883 4.5 19.9 1.0
OE2 A:GLU718 4.6 30.5 1.0
CB A:SER886 4.6 44.8 1.0
O A:ASP884 4.7 10.6 1.0
MG A:MG2007 4.8 30.2 1.0
C A:ASP884 4.9 10.6 1.0
CA A:ASP679 4.9 36.1 1.0
CB A:ASN722 4.9 35.0 1.0
N A:ASP884 5.0 10.6 1.0

Reference:

A.S.Tanwar, M.Morar, S.Panjikar, R.Anand. Formylglycinamide Ribonucleotide Amidotransferase From Salmonella Typhimurium: Role of Atp Complexation and the Glutaminase Domain in Catalytic Coupling Acta Crystallogr.,Sect.D V. 68 627 2012.
ISSN: ISSN 0907-4449
PubMed: 22683785
DOI: 10.1107/S0907444912006543
Page generated: Thu Aug 15 12:35:31 2024

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy