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Magnesium in PDB 7dw7: Crystal Structure of N1051A Mutant of Formylglycinamidine Synthetase

Enzymatic activity of Crystal Structure of N1051A Mutant of Formylglycinamidine Synthetase

All present enzymatic activity of Crystal Structure of N1051A Mutant of Formylglycinamidine Synthetase:
6.3.5.3;

Protein crystallography data

The structure of Crystal Structure of N1051A Mutant of Formylglycinamidine Synthetase, PDB code: 7dw7 was solved by N.Sharma, A.S.Tanwar, R.Anand, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 47.99 / 1.80
Space group P 65
Cell size a, b, c (Å), α, β, γ (°) 146.626, 146.626, 141.022, 90, 90, 120
R / Rfree (%) 13.3 / 16.3

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of N1051A Mutant of Formylglycinamidine Synthetase (pdb code 7dw7). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 3 binding sites of Magnesium where determined in the Crystal Structure of N1051A Mutant of Formylglycinamidine Synthetase, PDB code: 7dw7:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in 7dw7

Go back to Magnesium Binding Sites List in 7dw7
Magnesium binding site 1 out of 3 in the Crystal Structure of N1051A Mutant of Formylglycinamidine Synthetase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of N1051A Mutant of Formylglycinamidine Synthetase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1361

b:13.5
occ:1.00
O1B A:ADP1301 2.0 13.8 1.0
OD1 A:ASP884 2.0 12.9 1.0
OD1 A:ASP679 2.0 13.6 1.0
OD1 A:ASN722 2.1 12.6 1.0
O A:HOH2007 2.1 13.1 1.0
O A:HOH1632 2.2 12.4 1.0
CG A:ASP679 3.0 13.7 1.0
CG A:ASP884 3.0 12.8 1.0
CG A:ASN722 3.1 13.2 1.0
PB A:ADP1301 3.2 13.3 1.0
OD2 A:ASP884 3.4 14.3 1.0
ND2 A:ASN722 3.6 12.5 1.0
O3B A:ADP1301 3.7 12.3 1.0
O2B A:ADP1301 3.8 12.2 1.0
CB A:ASP679 3.9 12.9 1.0
OD2 A:ASP679 3.9 13.7 1.0
O A:HOH2023 4.0 14.1 1.0
OG A:SER886 4.1 14.4 1.0
NE2 A:HIS883 4.2 16.1 1.0
O A:HOH2265 4.3 19.7 1.0
CA A:ASP679 4.3 12.3 1.0
CD2 A:HIS883 4.4 10.8 1.0
CB A:ASP884 4.4 13.1 1.0
O A:ASP884 4.4 14.3 1.0
O A:HOH1470 4.4 13.8 1.0
CB A:ASN722 4.4 12.3 1.0
O3A A:ADP1301 4.5 13.4 1.0
N A:ASP884 4.6 12.3 1.0
CA A:ASN722 4.7 13.2 1.0
C A:ASP884 4.7 13.9 1.0
OE2 A:GLU718 4.8 14.2 1.0
CA A:ASP884 4.8 12.4 1.0
O A:ASP679 4.9 12.4 1.0
CB A:SER886 5.0 15.1 1.0

Magnesium binding site 2 out of 3 in 7dw7

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Magnesium binding site 2 out of 3 in the Crystal Structure of N1051A Mutant of Formylglycinamidine Synthetase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of N1051A Mutant of Formylglycinamidine Synthetase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1362

b:13.9
occ:1.00
O3B A:ADP1301 2.0 12.3 1.0
O A:HOH1463 2.1 14.1 1.0
O A:HOH1534 2.1 13.7 1.0
OE2 A:GLU718 2.1 14.2 1.0
O A:HOH1852 2.1 13.9 1.0
O A:HOH1748 2.1 12.5 1.0
CD A:GLU718 3.1 14.6 1.0
PB A:ADP1301 3.3 13.3 1.0
OE1 A:GLU718 3.5 15.1 1.0
O2B A:ADP1301 3.6 12.2 1.0
O A:HOH1632 4.0 12.4 1.0
O A:HOH1905 4.0 13.7 1.0
ND2 A:ASN722 4.1 12.5 1.0
O A:HOH1475 4.1 17.5 1.0
O3A A:ADP1301 4.2 13.4 1.0
O2A A:ADP1301 4.2 14.0 1.0
OE1 A:GLU699 4.3 17.5 1.0
OD2 A:ASP887 4.4 17.0 1.0
O A:ILE697 4.4 13.5 1.0
CG A:GLU718 4.4 12.8 1.0
O1B A:ADP1301 4.5 13.8 1.0
OG A:SER886 4.6 14.4 1.0
CB A:SER886 4.6 15.1 1.0
PA A:ADP1301 4.8 12.8 1.0
O A:GLU699 5.0 14.7 1.0
O A:HOH1933 5.0 12.3 1.0
N A:GLU699 5.0 13.5 1.0

Magnesium binding site 3 out of 3 in 7dw7

Go back to Magnesium Binding Sites List in 7dw7
Magnesium binding site 3 out of 3 in the Crystal Structure of N1051A Mutant of Formylglycinamidine Synthetase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Crystal Structure of N1051A Mutant of Formylglycinamidine Synthetase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1363

b:13.8
occ:1.00
O1A A:ADP1301 2.0 12.5 1.0
O2B A:ADP1301 2.0 12.2 1.0
O A:HOH1448 2.1 12.8 1.0
O A:HOH1776 2.1 13.5 1.0
O A:HOH1933 2.2 12.3 1.0
O A:HOH1470 2.2 13.8 1.0
PA A:ADP1301 3.2 12.8 1.0
PB A:ADP1301 3.3 13.3 1.0
O3A A:ADP1301 3.5 13.4 1.0
O2A A:ADP1301 3.9 14.0 1.0
O A:HOH1748 4.0 12.5 1.0
O A:HOH1987 4.0 16.6 1.0
OG A:SER886 4.1 14.4 1.0
O1B A:ADP1301 4.1 13.8 1.0
O A:HOH2007 4.1 13.1 1.0
OE2 A:GLU896 4.2 13.9 1.0
OE1 A:GLU896 4.2 13.8 1.0
O A:HOH2023 4.4 14.1 1.0
O3B A:ADP1301 4.4 12.3 1.0
O5' A:ADP1301 4.5 12.9 1.0
O A:THR645 4.5 15.2 1.0
OD2 A:ASP887 4.6 17.0 1.0
O A:HOH2341 4.6 14.7 1.0
O A:VAL646 4.6 13.1 1.0
CD A:GLU896 4.6 15.1 1.0
O A:ASP887 4.7 13.6 1.0
C5' A:ADP1301 4.8 13.8 1.0
CB A:ASP887 4.9 14.4 1.0
O A:HOH1534 5.0 13.7 1.0

Reference:

N.Sharma, S.Singh, A.S.Tanwar, J.Mondal, R.Anand. Mechanism of Coordinated Gating and Signal Transduction in Purine Biosynthetic Enzyme Formylglycinamidine Synthetase. Acs Catalysis V. 12 1930 2022.
ISSN: ESSN 2155-5435
DOI: 10.1021/ACSCATAL.1C05521
Page generated: Wed Oct 2 16:29:32 2024

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