Magnesium in PDB 6lyo: Crystal Structure of H296A Mutant of Formylglycinamidine Synthetase

Enzymatic activity of Crystal Structure of H296A Mutant of Formylglycinamidine Synthetase

All present enzymatic activity of Crystal Structure of H296A Mutant of Formylglycinamidine Synthetase:
6.3.5.3;

Protein crystallography data

The structure of Crystal Structure of H296A Mutant of Formylglycinamidine Synthetase, PDB code: 6lyo 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) 47.88 / 1.87
Space group P 65
Cell size a, b, c (Å), α, β, γ (°) 146.288, 146.288, 140.957, 90, 90, 120
R / Rfree (%) 12.5 / 15.8

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of H296A Mutant of Formylglycinamidine Synthetase (pdb code 6lyo). 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 H296A Mutant of Formylglycinamidine Synthetase, PDB code: 6lyo:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in 6lyo

Go back to Magnesium Binding Sites List in 6lyo
Magnesium binding site 1 out of 3 in the Crystal Structure of H296A 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 H296A Mutant of Formylglycinamidine Synthetase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1361

b:11.9
occ:1.00
OD1 A:ASP884 2.0 11.1 1.0
O3B A:ADP1301 2.0 11.8 1.0
OD1 A:ASP679 2.0 11.4 1.0
OD1 A:ASN722 2.1 10.9 1.0
O A:HOH1950 2.1 10.9 1.0
O A:HOH1530 2.2 12.1 1.0
CG A:ASP884 3.0 12.3 1.0
CG A:ASP679 3.0 12.5 1.0
CG A:ASN722 3.2 11.6 1.0
PB A:ADP1301 3.2 11.0 1.0
OD2 A:ASP884 3.3 12.0 1.0
ND2 A:ASN722 3.6 12.1 1.0
O1B A:ADP1301 3.7 10.8 1.0
CB A:ASP679 3.8 11.0 1.0
O2B A:ADP1301 3.8 10.7 1.0
OD2 A:ASP679 3.9 12.2 1.0
O A:HOH2019 4.0 11.7 1.0
OG A:SER886 4.1 12.5 1.0
NE2 A:HIS883 4.2 13.7 1.0
O A:HOH2214 4.2 19.5 1.0
CA A:ASP679 4.3 11.4 1.0
CD2 A:HIS883 4.3 10.3 1.0
CB A:ASP884 4.4 11.3 1.0
O A:ASP884 4.4 13.5 1.0
O A:HOH1477 4.5 11.4 1.0
CB A:ASN722 4.5 12.2 1.0
O3A A:ADP1301 4.5 11.7 1.0
N A:ASP884 4.6 10.8 1.0
CA A:ASN722 4.7 12.1 1.0
C A:ASP884 4.8 12.2 1.0
CA A:ASP884 4.8 11.3 1.0
OE2 A:GLU718 4.8 12.9 1.0
O A:ASP679 4.9 11.1 1.0
CB A:SER886 5.0 12.4 1.0

Magnesium binding site 2 out of 3 in 6lyo

Go back to Magnesium Binding Sites List in 6lyo
Magnesium binding site 2 out of 3 in the Crystal Structure of H296A 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 H296A Mutant of Formylglycinamidine Synthetase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1362

b:11.7
occ:1.00
O1B A:ADP1301 2.0 10.8 1.0
OE2 A:GLU718 2.0 12.9 1.0
O A:HOH1543 2.1 11.5 1.0
O A:HOH1756 2.1 12.2 1.0
O A:HOH1708 2.1 11.6 1.0
O A:HOH1537 2.1 11.8 1.0
CD A:GLU718 3.1 12.8 1.0
PB A:ADP1301 3.3 11.0 1.0
OE1 A:GLU718 3.5 12.4 1.0
O2B A:ADP1301 3.6 10.7 1.0
O A:HOH1785 4.0 11.0 1.0
O A:HOH1530 4.0 12.1 1.0
ND2 A:ASN722 4.1 12.1 1.0
O3A A:ADP1301 4.1 11.7 1.0
O1A A:ADP1301 4.2 12.8 1.0
O A:HOH1452 4.2 15.2 1.0
O A:ILE697 4.3 12.1 1.0
OE1 A:GLU699 4.3 16.6 1.0
OD2 A:ASP887 4.4 16.6 1.0
CG A:GLU718 4.4 11.7 1.0
O3B A:ADP1301 4.5 11.8 1.0
OG A:SER886 4.5 12.5 1.0
CB A:SER886 4.6 12.4 1.0
PA A:ADP1301 4.8 11.5 1.0
O A:GLU699 5.0 12.4 1.0
O A:HOH2007 5.0 11.7 1.0

Magnesium binding site 3 out of 3 in 6lyo

Go back to Magnesium Binding Sites List in 6lyo
Magnesium binding site 3 out of 3 in the Crystal Structure of H296A 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 H296A Mutant of Formylglycinamidine Synthetase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1363

b:12.1
occ:1.00
O2A A:ADP1301 2.0 11.8 1.0
O2B A:ADP1301 2.0 10.7 1.0
O A:HOH1477 2.1 11.4 1.0
O A:HOH1447 2.1 10.2 1.0
O A:HOH1732 2.2 12.0 1.0
O A:HOH2007 2.2 11.7 1.0
PA A:ADP1301 3.2 11.5 1.0
PB A:ADP1301 3.3 11.0 1.0
O3A A:ADP1301 3.5 11.7 1.0
O1A A:ADP1301 4.0 12.8 1.0
O A:HOH1756 4.1 12.2 1.0
O A:HOH2099 4.1 13.5 1.0
OG A:SER886 4.1 12.5 1.0
O3B A:ADP1301 4.1 11.8 1.0
OE2 A:GLU896 4.1 10.8 1.0
O A:HOH1950 4.1 10.9 1.0
OE1 A:GLU896 4.1 12.3 1.0
O A:HOH2019 4.4 11.7 1.0
O1B A:ADP1301 4.4 10.8 1.0
O5' A:ADP1301 4.5 10.9 1.0
O A:VAL646 4.6 11.2 1.0
O A:HOH2343 4.6 12.7 1.0
CD A:GLU896 4.6 12.9 1.0
O A:THR645 4.6 12.6 1.0
OD2 A:ASP887 4.6 16.6 1.0
O A:ASP887 4.7 12.1 1.0
C5' A:ADP1301 4.8 11.5 1.0
CB A:ASP887 5.0 13.3 1.0

Reference:

N.Sharma, A.S.Tanwar, R.Anand. Crystal Structure of H296A Mutant of Formylglycinamidine Synthetase To Be Published.
Page generated: Wed Mar 3 14:50:42 2021

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