Magnesium in PDB 7p4p: Structure of the Quinolinate Synthase A84L Variant Complexed with Citrate

Enzymatic activity of Structure of the Quinolinate Synthase A84L Variant Complexed with Citrate

All present enzymatic activity of Structure of the Quinolinate Synthase A84L Variant Complexed with Citrate:
2.5.1.72;

Protein crystallography data

The structure of Structure of the Quinolinate Synthase A84L Variant Complexed with Citrate, PDB code: 7p4p was solved by A.Volbeda, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 39.23 / 1.75
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 102.76, 49.2, 69.68, 90, 108.08, 90
R / Rfree (%) 17.1 / 20.2

Other elements in 7p4p:

The structure of Structure of the Quinolinate Synthase A84L Variant Complexed with Citrate also contains other interesting chemical elements:

Iron (Fe) 4 atoms
Chlorine (Cl) 3 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structure of the Quinolinate Synthase A84L Variant Complexed with Citrate (pdb code 7p4p). 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 Structure of the Quinolinate Synthase A84L Variant Complexed with Citrate, PDB code: 7p4p:

Magnesium binding site 1 out of 1 in 7p4p

Go back to Magnesium Binding Sites List in 7p4p
Magnesium binding site 1 out of 1 in the Structure of the Quinolinate Synthase A84L Variant Complexed with Citrate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of the Quinolinate Synthase A84L Variant Complexed with Citrate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg303

b:45.0
occ:1.00
 O A:THR271 2.5 38.3 1.0
O A:HOH635 2.7 43.0 1.0
C A:THR271 3.6 35.1 1.0
CB A:SER273 3.7 34.1 1.0
O A:GLU272 3.7 37.6 1.0
C A:GLU272 4.0 33.9 1.0
OG A:SER273 4.0 40.2 1.0
CB A:THR271 4.1 34.4 1.0
N A:SER273 4.3 34.7 1.0
CA A:THR271 4.3 37.3 1.0
CA A:SER273 4.5 33.5 1.0
OG1 A:THR271 4.6 38.6 1.0
N A:GLU272 4.6 33.3 1.0
CA A:GLU272 4.7 34.4 1.0

Reference:

H.Basbous, A.Volbeda, P.Amara, R.Rohac, L.Martin, S.Ollagnier De Choudens, J.C.Fontecilla-Camps. Essential Transient Extension of the Active Site Cavity During Quinolinic Acid Synthesis By Nada To Be Published.
Page generated: Fri Nov 5 15:33:30 2021

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