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Magnesium in PDB 1a82: Dethiobiotin Synthetase From Escherichia Coli, Complex with Substrates Atp and Diaminopelargonic Acid

Enzymatic activity of Dethiobiotin Synthetase From Escherichia Coli, Complex with Substrates Atp and Diaminopelargonic Acid

All present enzymatic activity of Dethiobiotin Synthetase From Escherichia Coli, Complex with Substrates Atp and Diaminopelargonic Acid:
6.3.3.3;

Protein crystallography data

The structure of Dethiobiotin Synthetase From Escherichia Coli, Complex with Substrates Atp and Diaminopelargonic Acid, PDB code: 1a82 was solved by H.Kaeck, K.J.Gibson, Y.Lindqvist, G.Schneider, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.80
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 72.900, 47.900, 60.900, 90.00, 106.50, 90.00
R / Rfree (%) 19 / 24.6

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Dethiobiotin Synthetase From Escherichia Coli, Complex with Substrates Atp and Diaminopelargonic Acid (pdb code 1a82). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Dethiobiotin Synthetase From Escherichia Coli, Complex with Substrates Atp and Diaminopelargonic Acid, PDB code: 1a82:

Magnesium binding site 1 out of 1 in 1a82

Go back to Magnesium Binding Sites List in 1a82
Magnesium binding site 1 out of 1 in the Dethiobiotin Synthetase From Escherichia Coli, Complex with Substrates Atp and Diaminopelargonic Acid


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Dethiobiotin Synthetase From Escherichia Coli, Complex with Substrates Atp and Diaminopelargonic Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg901

b:12.4
occ:1.00
 O1B A:ATP802 2.0 7.3 1.0
OE2 A:GLU115 2.1 6.4 1.0
OD2 A:ASP54 2.2 4.4 1.0
OG1 A:THR16 2.2 4.0 1.0
O3G A:ATP802 2.2 16.2 1.0
O A:HOH444 2.4 10.8 1.0
CG A:ASP54 3.0 4.0 1.0
CD A:GLU115 3.1 7.9 1.0
PB A:ATP802 3.2 8.3 1.0
PG A:ATP802 3.3 23.5 1.0
CB A:THR16 3.3 6.8 1.0
O3B A:ATP802 3.4 13.3 1.0
OD1 A:ASP54 3.5 5.4 1.0
OE1 A:GLU115 3.5 7.7 1.0
N A:THR16 3.7 4.3 1.0
NZ A:LYS37 3.9 5.1 1.0
O1G A:ATP802 3.9 19.6 1.0
CA A:THR16 4.0 4.8 1.0
CB A:ASP54 4.1 5.9 1.0
O2A A:ATP802 4.2 10.5 1.0
O3A A:ATP802 4.2 9.6 1.0
O2B A:ATP802 4.2 8.3 1.0
CB A:LYS15 4.3 5.0 1.0
O A:HOH716 4.3 13.0 1.0
O2G A:ATP802 4.4 20.8 1.0
CG A:GLU115 4.4 5.8 1.0
CE A:LYS15 4.5 6.4 1.0
CG2 A:THR16 4.5 3.8 1.0
PA A:ATP802 4.6 11.6 1.0
C A:LYS15 4.6 4.6 1.0
O A:HOH717 4.6 15.8 1.0
NZ A:LYS15 4.7 7.8 1.0
O1A A:ATP802 4.8 11.3 1.0
CA A:LYS15 4.9 5.4 1.0
CE A:LYS37 5.0 5.9 1.0

Reference:

H.Kack, K.J.Gibson, Y.Lindqvist, G.Schneider. Snapshot of A Phosphorylated Substrate Intermediate By Kinetic Crystallography. Proc.Natl.Acad.Sci.Usa V. 95 5495 1998.
ISSN: ISSN 0027-8424
PubMed: 9576910
DOI: 10.1073/PNAS.95.10.5495
Page generated: Tue Aug 13 02:01:09 2024

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