Calcium in PDB 8a8d: Atp Sulfurylase From Methanothermococcus Thermolithotrophicus - Monoclinic Form

All present enzymatic activity of Atp Sulfurylase From Methanothermococcus Thermolithotrophicus - Monoclinic Form:
2.7.7.4;

The structure of Atp Sulfurylase From Methanothermococcus Thermolithotrophicus - Monoclinic Form, PDB code: 8a8d was solved by M.Jespersen, T.Wagner, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	52.28 / 2.10
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	185.282, 54.525, 85.43, 90, 95.91, 90
R / Rfree (%)	19.9 / 23.9

The structure of Atp Sulfurylase From Methanothermococcus Thermolithotrophicus - Monoclinic Form also contains other interesting chemical elements:

Zinc

(Zn)

2 atoms

The binding sites of Calcium atom in the Atp Sulfurylase From Methanothermococcus Thermolithotrophicus - Monoclinic Form (pdb code 8a8d). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 3 binding sites of Calcium where determined in the Atp Sulfurylase From Methanothermococcus Thermolithotrophicus - Monoclinic Form, PDB code: 8a8d:
Jump to Calcium binding site number: 1; 2; 3;

Calcium binding site 1 out of 3 in the Atp Sulfurylase From Methanothermococcus Thermolithotrophicus - Monoclinic Form


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Atp Sulfurylase From Methanothermococcus Thermolithotrophicus - Monoclinic Form within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca412 b:49.9 occ:1.00 O A:LEU145 2.3 43.4 1.0 O A:HOH655 2.4 42.9 1.0 O A:ACT410 2.5 64.8 1.0 O A:TYR143 2.7 35.8 1.0 O A:HOH562 2.9 37.2 1.0 C A:ACT410 3.1 60.7 1.0 OXT A:ACT410 3.1 50.6 1.0 C A:LEU145 3.5 39.0 1.0 C A:TYR143 3.8 35.3 1.0 N A:LEU145 4.0 35.5 1.0 C A:ALA144 4.1 41.2 1.0 CA A:LEU145 4.3 37.0 1.0 O A:ALA144 4.4 38.0 1.0 C A:GLY146 4.4 44.1 1.0 N A:GLY146 4.5 44.8 1.0 O A:GLY146 4.5 39.5 1.0 CH3 A:ACT410 4.6 59.1 1.0 CA A:GLY146 4.6 46.8 1.0 OH A:TYR119 4.6 46.5 1.0 CA A:ALA144 4.6 37.3 1.0 N A:ALA144 4.7 39.2 1.0 CA A:TYR143 4.7 39.2 1.0 CD A:LYS121 4.8 44.3 1.0 N A:GLU147 4.9 47.4 1.0 O A:THR142 4.9 37.6 1.0 CB A:LEU145 4.9 35.6 1.0

Calcium binding site 2 out of 3 in the Atp Sulfurylase From Methanothermococcus Thermolithotrophicus - Monoclinic Form


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Atp Sulfurylase From Methanothermococcus Thermolithotrophicus - Monoclinic Form within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca406 b:47.8 occ:1.00 OE2 B:GLU95 2.3 59.3 1.0 OXT B:ACT402 2.4 51.2 1.0 O B:ACT402 2.4 55.9 1.0 O B:HOH519 2.5 56.6 1.0 OE1 B:GLU95 2.5 53.3 1.0 C B:ACT402 2.6 63.5 1.0 CD B:GLU95 2.7 57.5 1.0 O B:HOH542 3.0 46.5 1.0 O B:HOH557 3.1 53.9 1.0 CB B:GLU115 3.8 60.5 1.0 CH3 B:ACT402 4.1 65.0 1.0 CG B:GLU95 4.2 51.3 1.0 CA B:GLU115 4.4 53.0 1.0 OE1 B:GLU115 4.8 57.8 1.0 N B:ILE116 4.8 45.8 1.0 O B:ILE116 4.9 49.0 1.0 CG B:GLU115 5.0 50.5 1.0 O B:ASP114 5.0 41.5 1.0

Calcium binding site 3 out of 3 in the Atp Sulfurylase From Methanothermococcus Thermolithotrophicus - Monoclinic Form


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 3 of Atp Sulfurylase From Methanothermococcus Thermolithotrophicus - Monoclinic Form within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca407 b:55.0 occ:1.00 O B:HOH554 2.3 45.8 1.0 O B:HOH561 2.4 55.2 1.0 O B:HOH631 2.4 58.1 1.0 OE1 B:GLU147 2.4 72.6 1.0 O B:LEU145 2.5 47.5 1.0 O B:TYR143 2.6 40.4 1.0 CD B:GLU147 3.6 80.5 1.0 C B:LEU145 3.7 47.0 1.0 C B:TYR143 3.8 40.6 1.0 N B:LEU145 4.2 43.2 1.0 C B:ALA144 4.3 43.8 1.0 OE2 B:GLU147 4.3 65.3 1.0 CD B:LYS121 4.5 56.4 1.0 CA B:LEU145 4.6 43.0 1.0 CA B:TYR143 4.6 43.0 1.0 CA B:ALA144 4.6 44.2 1.0 C B:GLY146 4.7 44.6 1.0 N B:ALA144 4.7 43.1 1.0 O B:ALA144 4.7 45.4 1.0 CG B:GLU147 4.7 67.5 1.0 OH B:TYR119 4.7 39.7 1.0 N B:GLY146 4.7 47.6 1.0 CA B:GLY146 4.8 47.7 1.0 N B:GLU147 4.9 49.6 1.0 O B:GLY146 4.9 46.1 1.0 O B:THR142 5.0 42.9 1.0

M.Jespersen, T.Wagner. How A Methanogen Assimilates Sulfate: Structural and Functional Elucidation of the Complete Sulfate-Reduction Pathway. To Be Published.