Magnesium in PDB 7kwn: Dihydrodipicolinate Synthase From C. Jejuni with Pyruvate Bound to the Active Site in C2221 Space Group

Enzymatic activity of Dihydrodipicolinate Synthase From C. Jejuni with Pyruvate Bound to the Active Site in C2221 Space Group

All present enzymatic activity of Dihydrodipicolinate Synthase From C. Jejuni with Pyruvate Bound to the Active Site in C2221 Space Group:
4.3.3.7;

Protein crystallography data

The structure of Dihydrodipicolinate Synthase From C. Jejuni with Pyruvate Bound to the Active Site in C2221 Space Group, PDB code: 7kwn 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) 45.89 / 2.24
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 83.99, 230.19, 200.14, 90, 90, 90
R / Rfree (%) 17.7 / 21.6

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Dihydrodipicolinate Synthase From C. Jejuni with Pyruvate Bound to the Active Site in C2221 Space Group (pdb code 7kwn). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Dihydrodipicolinate Synthase From C. Jejuni with Pyruvate Bound to the Active Site in C2221 Space Group, PDB code: 7kwn:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 7kwn

Go back to Magnesium Binding Sites List in 7kwn
Magnesium binding site 1 out of 2 in the Dihydrodipicolinate Synthase From C. Jejuni with Pyruvate Bound to the Active Site in C2221 Space Group


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Dihydrodipicolinate Synthase From C. Jejuni with Pyruvate Bound to the Active Site in C2221 Space Group within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg306

b:30.0
occ:1.00
ND2 B:ASN252 3.6 23.1 1.0
NE B:ARG142 3.6 46.6 1.0
OH B:TYR137 4.1 32.1 1.0
CE2 B:PHE248 4.2 31.8 1.0
CD B:ARG142 4.3 41.9 1.0
NH2 B:ARG142 4.3 46.5 1.0
CZ B:ARG142 4.3 43.8 1.0
CB B:ASN252 4.3 31.4 1.0
CG B:ASN252 4.4 28.6 1.0
C1 B:KPI166 4.5 34.2 1.0
CG2 B:THR47 4.5 31.8 1.0
CB B:THR47 4.7 31.9 1.0
CZ B:PHE248 4.7 34.2 1.0
O1 B:KPI166 4.9 25.7 1.0

Magnesium binding site 2 out of 2 in 7kwn

Go back to Magnesium Binding Sites List in 7kwn
Magnesium binding site 2 out of 2 in the Dihydrodipicolinate Synthase From C. Jejuni with Pyruvate Bound to the Active Site in C2221 Space Group


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Dihydrodipicolinate Synthase From C. Jejuni with Pyruvate Bound to the Active Site in C2221 Space Group within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg307

b:30.0
occ:1.00
N B:VAL107 3.1 27.5 1.0
O B:LEU105 3.2 31.6 1.0
N B:GLY82 3.2 45.2 1.0
CG1 B:VAL107 3.4 26.2 1.0
O D:HOH445 3.6 47.4 1.0
CB B:VAL107 3.6 29.2 1.0
O B:HOH448 3.6 46.0 1.0
CA B:GLY82 3.6 42.2 1.0
N B:ALA81 3.7 36.0 1.0
CA B:SER106 3.9 26.4 1.0
C B:LEU105 3.9 30.2 1.0
CA B:VAL107 4.0 27.8 1.0
C B:SER106 4.0 27.1 1.0
C B:ALA81 4.1 47.1 1.0
N B:SER106 4.2 27.6 1.0
CA B:GLY80 4.2 33.4 1.0
C B:GLY80 4.3 33.9 1.0
CA B:ALA81 4.5 40.0 1.0
C B:GLY82 4.5 36.3 1.0
CD2 B:TYR137 4.6 30.4 1.0
O B:GLY82 4.8 37.6 1.0
CG B:LEU105 4.8 26.6 1.0
CG2 B:VAL107 5.0 28.5 1.0

Reference:

S.Saran, D.A.R.Sanders. B-Factor Analysis Suggest That L-Lysine and R, R-Bislysine Allosterically Inhibit Cj.Dhdps Enzyme By Decreasing Protein Dynamics. To Be Published.
Page generated: Fri Dec 17 10:33:05 2021

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