Magnesium in PDB 7kto: Dihydrodipicolinate Synthase (Dhdps) From C.Jejuni, H56A Mutant with Pyruvate Bound in the Active Site and R,R-Bislysine Bound at the Allosteric Site

Enzymatic activity of Dihydrodipicolinate Synthase (Dhdps) From C.Jejuni, H56A Mutant with Pyruvate Bound in the Active Site and R,R-Bislysine Bound at the Allosteric Site

All present enzymatic activity of Dihydrodipicolinate Synthase (Dhdps) From C.Jejuni, H56A Mutant with Pyruvate Bound in the Active Site and R,R-Bislysine Bound at the Allosteric Site:
4.3.3.7;

Protein crystallography data

The structure of Dihydrodipicolinate Synthase (Dhdps) From C.Jejuni, H56A Mutant with Pyruvate Bound in the Active Site and R,R-Bislysine Bound at the Allosteric Site, PDB code: 7kto was solved by S.Saran, D.A.R.Sanders, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 45.83 / 2.13
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 85.08, 225.15, 200.73, 90, 90, 90
R / Rfree (%) 20.2 / 24.7

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Dihydrodipicolinate Synthase (Dhdps) From C.Jejuni, H56A Mutant with Pyruvate Bound in the Active Site and R,R-Bislysine Bound at the Allosteric Site (pdb code 7kto). 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 Dihydrodipicolinate Synthase (Dhdps) From C.Jejuni, H56A Mutant with Pyruvate Bound in the Active Site and R,R-Bislysine Bound at the Allosteric Site, PDB code: 7kto:

Magnesium binding site 1 out of 1 in 7kto

Go back to Magnesium Binding Sites List in 7kto
Magnesium binding site 1 out of 1 in the Dihydrodipicolinate Synthase (Dhdps) From C.Jejuni, H56A Mutant with Pyruvate Bound in the Active Site and R,R-Bislysine Bound at the Allosteric Site


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Dihydrodipicolinate Synthase (Dhdps) From C.Jejuni, H56A Mutant with Pyruvate Bound in the Active Site and R,R-Bislysine Bound at the Allosteric Site within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Mg306

b:41.5
occ:1.00
 O C:HOH549 2.6 39.6 1.0
OE1 E:GLU287 2.8 35.3 1.0
O E:LEU262 3.0 30.8 1.0
N C:HIS-4 3.1 30.3 1.0
OE2 E:GLU287 3.4 33.3 1.0
CD E:GLU287 3.5 33.5 1.0
CD2 C:HIS-4 3.5 31.6 1.0
CA C:HIS-5 3.5 33.8 1.0
CD2 C:HIS-3 3.5 28.1 1.0
CB C:HIS-5 3.5 33.8 1.0
NE2 C:HIS-3 3.7 28.3 1.0
C C:HIS-5 3.8 32.3 1.0
CB C:HIS-4 3.9 30.8 1.0
CG C:HIS-4 3.9 31.1 1.0
CD2 E:LEU262 3.9 29.0 1.0
C E:LEU262 4.0 28.0 1.0
CA C:HIS-4 4.0 29.9 1.0
CA E:LEU262 4.3 25.6 1.0
CB E:LEU262 4.4 25.8 1.0
O E:HOH581 4.4 37.8 1.0
NE2 C:HIS-4 4.6 31.9 1.0
C C:HIS-4 4.8 29.2 1.0
CG C:HIS-3 4.8 28.0 1.0
CG C:HIS-5 4.8 34.1 1.0
O C:HIS-6 4.8 39.9 1.0
CG E:LEU262 4.8 27.2 1.0
N C:HIS-5 4.9 36.2 1.0
CG E:GLU287 4.9 31.9 1.0
O E:HOH604 4.9 42.7 1.0
CE1 C:HIS-3 4.9 28.5 1.0
N C:HIS-3 5.0 29.2 1.0

Reference:

S.Saran, Y.Skovpen, M.M.Yazdi, D.R.J.Palmer, D.A.R.Sanders. Allosteric Site Residue 'H56' Caps the Inhibitor at the Tight Dimer Interface For Transmitting the Allosteric Inhibition Signals in Cj.Dhdps To Be Published.
Page generated: Fri Dec 17 10:32:45 2021

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