Magnesium in PDB 8vsy: Bile Salt Hydrolase From Arthrobacter Citreus with Covalent Inhibitor Aaa-10 Bound

The structure of Bile Salt Hydrolase From Arthrobacter Citreus with Covalent Inhibitor Aaa-10 Bound, PDB code: 8vsy was solved by P.Dhindwal, A.Ruzzini, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	42.95 / 1.60
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	167.76, 43.84, 87.16, 90, 111.02, 90
R / Rfree (%)	13.6 / 15.7

The structure of Bile Salt Hydrolase From Arthrobacter Citreus with Covalent Inhibitor Aaa-10 Bound also contains other interesting chemical elements:

Chlorine

(Cl)

1 atom

The binding sites of Magnesium atom in the Bile Salt Hydrolase From Arthrobacter Citreus with Covalent Inhibitor Aaa-10 Bound (pdb code 8vsy). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 5 binding sites of Magnesium where determined in the Bile Salt Hydrolase From Arthrobacter Citreus with Covalent Inhibitor Aaa-10 Bound, PDB code: 8vsy:
Jump to Magnesium binding site number: 1; 2; 3; 4; 5;

Magnesium binding site 1 out of 5 in the Bile Salt Hydrolase From Arthrobacter Citreus with Covalent Inhibitor Aaa-10 Bound


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Bile Salt Hydrolase From Arthrobacter Citreus with Covalent Inhibitor Aaa-10 Bound within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg401 b:34.2 occ:1.00 O A:HOH713 1.8 52.8 1.0 O A:HOH508 2.1 32.0 1.0 O A:HOH820 2.1 51.5 1.0 O A:HOH818 2.1 42.2 1.0 O A:HOH506 2.2 39.1 1.0 O A:HOH568 2.4 28.8 1.0 OD1 A:ASP25 3.3 57.1 1.0 CG A:ASP25 3.8 36.1 1.0 OE2 A:GLU28 3.9 28.9 1.0 OE1 A:GLU293 4.1 20.6 1.0 CB A:ASP25 4.1 34.9 1.0 O A:HOH574 4.3 35.2 1.0 O A:THR275 4.4 11.7 1.0 O A:HOH599 4.4 40.4 1.0 OD2 A:ASP25 4.5 71.7 1.0 CG2 A:THR291 4.7 13.7 1.0 O A:HOH737 4.7 35.2 1.0 CD A:GLU28 4.8 31.4 1.0 CD A:GLU293 4.9 37.7 1.0 CB A:THR291 4.9 11.2 1.0 OE2 A:GLU293 4.9 45.9 1.0

Magnesium binding site 2 out of 5 in the Bile Salt Hydrolase From Arthrobacter Citreus with Covalent Inhibitor Aaa-10 Bound


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Bile Salt Hydrolase From Arthrobacter Citreus with Covalent Inhibitor Aaa-10 Bound within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg402 b:65.1 occ:1.00 O A:HOH798 2.3 55.2 1.0 O A:HOH601 2.6 53.4 1.0 O A:HOH616 4.4 37.9 1.0 O A:HOH730 4.6 24.3 1.0 OD2 A:ASP308 4.8 31.5 1.0 CB A:ASP308 4.9 32.7 1.0

Magnesium binding site 3 out of 5 in the Bile Salt Hydrolase From Arthrobacter Citreus with Covalent Inhibitor Aaa-10 Bound


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Bile Salt Hydrolase From Arthrobacter Citreus with Covalent Inhibitor Aaa-10 Bound within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg403 b:34.5 occ:1.00 O A:HOH664 2.1 19.5 1.0 O A:HOH862 2.2 41.3 1.0 O A:HOH800 2.3 31.7 1.0 O A:HOH700 3.9 18.9 1.0 O A:HOH640 4.0 34.7 1.0 O A:HOH663 4.1 33.2 1.0 O A:THR39 4.2 16.4 1.0 O A:HOH643 4.6 16.9 1.0 O A:HOH861 4.6 18.7 1.0 CG2 A:THR38 4.6 20.1 1.0

Magnesium binding site 4 out of 5 in the Bile Salt Hydrolase From Arthrobacter Citreus with Covalent Inhibitor Aaa-10 Bound


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Bile Salt Hydrolase From Arthrobacter Citreus with Covalent Inhibitor Aaa-10 Bound within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg404 b:47.5 occ:1.00 O A:HOH549 2.3 45.8 1.0 O A:HOH554 2.5 18.2 1.0 O A:HOH575 2.6 21.8 1.0 O A:HOH755 2.6 33.4 1.0 O B:HOH734 3.6 34.7 1.0 OD1 A:ASN173 3.7 13.0 1.0 CG A:ASN173 3.8 10.5 1.0 OE1 A:GLN174 4.0 20.7 1.0 CB A:ASN173 4.0 9.4 1.0 O A:HOH697 4.3 14.8 1.0 ND2 A:ASN173 4.3 11.3 1.0 NH2 A:ARG226 4.5 11.2 1.0 CA B:GLY209 4.5 11.7 1.0 OE2 A:GLU272 4.6 17.1 0.5 O A:HOH677 4.6 14.2 1.0 OE2 A:GLU272 4.6 28.8 0.5 OE1 A:GLU272 4.6 18.1 0.5 NE2 A:GLN174 4.7 22.1 1.0 OE1 A:GLU272 4.8 14.9 0.5 O B:PHE208 4.8 16.6 1.0 CD A:GLN174 4.8 18.9 1.0

Magnesium binding site 5 out of 5 in the Bile Salt Hydrolase From Arthrobacter Citreus with Covalent Inhibitor Aaa-10 Bound


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 5 of Bile Salt Hydrolase From Arthrobacter Citreus with Covalent Inhibitor Aaa-10 Bound within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg401 b:35.0 occ:1.00 O B:HOH513 2.0 50.5 1.0 O B:HOH816 2.0 44.8 1.0 O B:HOH506 2.2 26.9 0.5 O B:HOH505 2.2 36.1 1.0 O B:HOH522 2.3 29.4 1.0 O B:HOH792 2.4 65.8 1.0 O3 B:GOL402 3.5 31.9 1.0 CB B:ASP25 3.8 49.6 1.0 OD2 B:ASP25 3.9 48.9 1.0 OE1 B:GLU293 4.1 21.6 1.0 OE2 B:GLU28 4.1 30.5 1.0 CG B:ASP25 4.2 53.7 1.0 O B:HOH621 4.2 31.1 0.6 O2 B:GOL402 4.2 54.7 1.0 O B:THR275 4.3 10.5 1.0 C3 B:GOL402 4.6 24.8 1.0 C2 B:GOL402 4.7 33.1 1.0 CG2 B:THR291 4.7 14.1 1.0 O B:HOH716 4.7 31.7 1.0 CB B:THR291 4.9 12.7 1.0 CD B:GLU293 5.0 33.7 1.0 O B:HOH650 5.0 32.0 1.0

P.Dhindwal, A.Ruzzini. Bile Salt Hydrolase From Arthrobacter Citreus with Covalent Inhibitor Aaa-10 Bound To Be Published.