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Magnesium in PDB 5bur: O-Succinylbenzoate Coenzyme A Synthetase (Mene) From Bacillus Subtilis, in Complex with Atp and Magnesium Ion

Enzymatic activity of O-Succinylbenzoate Coenzyme A Synthetase (Mene) From Bacillus Subtilis, in Complex with Atp and Magnesium Ion

All present enzymatic activity of O-Succinylbenzoate Coenzyme A Synthetase (Mene) From Bacillus Subtilis, in Complex with Atp and Magnesium Ion:
6.2.1.26;

Protein crystallography data

The structure of O-Succinylbenzoate Coenzyme A Synthetase (Mene) From Bacillus Subtilis, in Complex with Atp and Magnesium Ion, PDB code: 5bur was solved by Y.Chen, Y.Sun, H.Song, Z.Guo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 36.39 / 2.82
Space group P 43
Cell size a, b, c (Å), α, β, γ (°) 121.835, 121.835, 97.801, 90.00, 90.00, 90.00
R / Rfree (%) 20.4 / 25.2

Other elements in 5bur:

The structure of O-Succinylbenzoate Coenzyme A Synthetase (Mene) From Bacillus Subtilis, in Complex with Atp and Magnesium Ion also contains other interesting chemical elements:

Chlorine (Cl) 6 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the O-Succinylbenzoate Coenzyme A Synthetase (Mene) From Bacillus Subtilis, in Complex with Atp and Magnesium Ion (pdb code 5bur). 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 O-Succinylbenzoate Coenzyme A Synthetase (Mene) From Bacillus Subtilis, in Complex with Atp and Magnesium Ion, PDB code: 5bur:

Magnesium binding site 1 out of 1 in 5bur

Go back to Magnesium Binding Sites List in 5bur
Magnesium binding site 1 out of 1 in the O-Succinylbenzoate Coenzyme A Synthetase (Mene) From Bacillus Subtilis, in Complex with Atp and Magnesium Ion


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of O-Succinylbenzoate Coenzyme A Synthetase (Mene) From Bacillus Subtilis, in Complex with Atp and Magnesium Ion within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg505

b:64.3
occ:1.00
 O A:HOH603 1.9 51.0 1.0
O2G A:ATP506 2.1 59.7 1.0
O2B A:ATP506 2.4 59.0 1.0
O A:HOH601 2.8 44.3 1.0
O A:HOH611 2.9 66.6 1.0
PG A:ATP506 3.5 75.3 1.0
PB A:ATP506 3.6 69.1 1.0
O3' A:ATP506 3.8 66.2 1.0
O3B A:ATP506 4.0 73.6 1.0
NH1 A:ARG382 4.0 74.0 1.0
O A:HOH619 4.1 51.0 1.0
O A:THR365 4.1 56.6 1.0
O1G A:ATP506 4.2 68.4 1.0
O1B A:ATP506 4.2 72.5 1.0
CE A:MET288 4.4 58.7 1.0
OE2 A:GLU290 4.6 52.3 1.0
O1A A:ATP506 4.6 56.0 1.0
NZ A:LYS160 4.6 66.5 1.0
O3G A:ATP506 4.6 67.6 1.0
O3A A:ATP506 4.9 66.0 1.0
C3' A:ATP506 5.0 63.7 1.0
C4' A:ATP506 5.0 60.8 1.0
OE1 A:GLU290 5.0 47.3 1.0

Reference:

Y.Chen, Y.Sun, H.Song, Z.Guo. Structural Basis For the Atp-Dependent Configuration of Adenylation Active Site in Bacillus Subtilis O-Succinylbenzoyl-Coa Synthetase J.Biol.Chem. V. 290 23971 2015.
ISSN: ESSN 1083-351X
PubMed: 26276389
DOI: 10.1074/JBC.M115.676304
Page generated: Sun Sep 29 01:44:54 2024

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