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Magnesium in PDB 6znw: Methanosaeta Concilii Atp Citrate Lyase (D541A Mutant) in Complex with (3S)-Citryl-Coa.

Enzymatic activity of Methanosaeta Concilii Atp Citrate Lyase (D541A Mutant) in Complex with (3S)-Citryl-Coa.

All present enzymatic activity of Methanosaeta Concilii Atp Citrate Lyase (D541A Mutant) in Complex with (3S)-Citryl-Coa.:
2.3.3.8;

Protein crystallography data

The structure of Methanosaeta Concilii Atp Citrate Lyase (D541A Mutant) in Complex with (3S)-Citryl-Coa., PDB code: 6znw was solved by K.H.G.Verschueren, K.Verstraete, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 79.04 / 2.12
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 73.531, 154.373, 276.054, 90, 90, 90
R / Rfree (%) 18.6 / 20.3

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Methanosaeta Concilii Atp Citrate Lyase (D541A Mutant) in Complex with (3S)-Citryl-Coa. (pdb code 6znw). 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 Methanosaeta Concilii Atp Citrate Lyase (D541A Mutant) in Complex with (3S)-Citryl-Coa., PDB code: 6znw:

Magnesium binding site 1 out of 1 in 6znw

Go back to Magnesium Binding Sites List in 6znw
Magnesium binding site 1 out of 1 in the Methanosaeta Concilii Atp Citrate Lyase (D541A Mutant) in Complex with (3S)-Citryl-Coa.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Methanosaeta Concilii Atp Citrate Lyase (D541A Mutant) in Complex with (3S)-Citryl-Coa. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg502

b:114.0
occ:1.00
O A:HOH611 2.0 98.3 1.0
O B:HOH856 2.1 73.4 1.0
OG2 A:FLC501 2.1 78.2 1.0
O1 A:PO4503 2.1 107.3 1.0
OG A:SER306 2.1 84.8 1.0
O A:HOH610 2.2 97.9 1.0
CB A:SER306 3.1 82.2 1.0
CGC A:FLC501 3.2 78.1 1.0
P A:PO4503 3.4 107.2 1.0
OG1 A:FLC501 3.7 78.5 1.0
O3 A:PO4503 3.8 107.5 1.0
O4 A:PO4503 3.9 106.6 1.0
HA2 A:FLC501 4.1 91.3 0.0
OE2 B:GLU114 4.1 95.4 1.0
OE2 A:GLU304 4.1 100.4 1.0
HOB A:FLC501 4.3 91.4 0.0
CA A:SER306 4.3 81.4 1.0
OE1 A:GLU304 4.4 99.6 1.0
N A:GLY280 4.4 87.3 1.0
CG A:FLC501 4.5 77.3 1.0
N A:GLY307 4.5 80.3 1.0
CD B:GLU114 4.5 96.9 1.0
C A:SER306 4.6 81.0 1.0
CB A:SER261 4.6 91.4 1.0
HG2 A:FLC501 4.6 92.8 0.0
OE1 B:GLU114 4.6 101.2 1.0
O2 A:PO4503 4.6 107.1 1.0
CA A:GLY279 4.7 87.2 1.0
CD A:GLU304 4.7 98.5 1.0
OHB A:FLC501 4.9 76.2 1.0

Reference:

K.H.G.Verschueren, K.Verstraete. Structural Basis of Acetyl-Coa Production By the Citrate Synthase Homology Module of Atp-Citrate Lyase To Be Published.
Page generated: Wed Oct 2 02:28:34 2024

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