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Magnesium in PDB 1wxe: E.Coli Nad Synthetase, Amp

Enzymatic activity of E.Coli Nad Synthetase, Amp

All present enzymatic activity of E.Coli Nad Synthetase, Amp:
6.3.1.5;

Protein crystallography data

The structure of E.Coli Nad Synthetase, Amp, PDB code: 1wxe was solved by R.Jauch, A.Humm, R.Huber, M.C.Wahl, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 1.90
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 92.450, 67.820, 48.282, 90.00, 104.47, 90.00
R / Rfree (%) 19.1 / 21.1

Magnesium Binding Sites:

The binding sites of Magnesium atom in the E.Coli Nad Synthetase, Amp (pdb code 1wxe). 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 E.Coli Nad Synthetase, Amp, PDB code: 1wxe:

Magnesium binding site 1 out of 1 in 1wxe

Go back to Magnesium Binding Sites List in 1wxe
Magnesium binding site 1 out of 1 in the E.Coli Nad Synthetase, Amp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of E.Coli Nad Synthetase, Amp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg300

b:42.9
occ:1.00
O A:HOH637 2.4 37.8 1.0
OD2 A:ASP52 2.4 15.1 1.0
OE2 A:GLU165 2.4 20.7 1.0
O A:HOH569 2.4 21.5 1.0
O A:HOH640 2.5 45.1 1.0
O A:HOH581 2.5 25.5 1.0
CG A:ASP52 3.3 12.7 1.0
CD A:GLU165 3.4 21.2 1.0
O A:HOH539 3.6 24.4 1.0
OE1 A:GLU165 3.7 21.3 1.0
CB A:ASP52 3.7 12.5 1.0
O5' A:AMP400 3.7 53.6 1.0
O1P A:AMP400 3.8 55.9 1.0
C5' A:AMP400 4.1 48.7 1.0
O A:HOH580 4.3 19.2 1.0
O3' A:AMP400 4.3 43.7 1.0
OG1 A:THR160 4.4 14.7 1.0
OD1 A:ASP52 4.4 14.8 1.0
P A:AMP400 4.5 56.0 1.0
O A:HOH519 4.5 24.1 1.0
O A:HOH543 4.5 25.4 1.0
O A:HOH638 4.7 50.4 1.0
NZ A:LYS189 4.7 14.2 1.0
O A:HOH582 4.7 27.6 1.0
CG A:GLU165 4.8 17.6 1.0
NE2 A:HIS162 4.8 17.7 1.0
C3' A:AMP400 4.9 44.7 1.0
C4' A:AMP400 4.9 45.9 1.0

Reference:

R.Jauch, A.Humm, R.Huber, M.C.Wahl. Structures of Escherichia Coli Nad Synthetase with Substrates and Products Reveal Mechanistic Rearrangements J.Biol.Chem. V. 280 15131 2005.
ISSN: ISSN 0021-9258
PubMed: 15699042
DOI: 10.1074/JBC.M413195200
Page generated: Mon Dec 14 07:02:32 2020

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