Zinc 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:

Calcium

(Ca)

3 atoms

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

Zinc binding site 1 out of 2 in the Atp Sulfurylase From Methanothermococcus Thermolithotrophicus - Monoclinic Form


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Atp Sulfurylase From Methanothermococcus Thermolithotrophicus - Monoclinic Form within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn401 b:19.9 occ:1.00 ND1 A:HIS336 2.0 22.2 1.0 SG A:CYS334 2.3 24.4 1.0 SG A:CYS325 2.3 25.9 1.0 SG A:CYS322 2.4 22.8 1.0 CE1 A:HIS336 3.0 27.3 1.0 CG A:HIS336 3.1 29.0 1.0 CB A:CYS322 3.3 21.3 1.0 CB A:CYS334 3.4 24.7 1.0 CB A:CYS325 3.4 22.3 1.0 CB A:HIS336 3.5 28.9 1.0 N A:CYS325 3.8 22.6 1.0 NE2 A:HIS336 4.1 33.2 1.0 CA A:CYS334 4.1 19.6 1.0 CD2 A:HIS336 4.2 27.4 1.0 CA A:CYS325 4.2 18.2 1.0 N A:HIS336 4.4 26.8 1.0 CD A:PRO335 4.4 23.4 1.0 CG2 A:VAL329 4.5 21.2 1.0 CA A:HIS336 4.6 24.5 1.0 C A:CYS334 4.6 22.8 1.0 N A:PRO335 4.7 22.7 1.0 CA A:CYS322 4.7 23.6 1.0 CB A:LYS324 4.8 25.4 1.0 O B:HOH563 4.8 19.5 1.0 C A:LYS324 4.9 22.9 1.0

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


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Atp Sulfurylase From Methanothermococcus Thermolithotrophicus - Monoclinic Form within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn401 b:22.8 occ:1.00 ND1 B:HIS336 2.1 23.9 1.0 SG B:CYS322 2.3 22.3 1.0 SG B:CYS334 2.3 24.6 1.0 SG B:CYS325 2.4 23.9 1.0 CE1 B:HIS336 2.8 24.9 1.0 CG B:HIS336 3.2 25.2 1.0 CB B:CYS322 3.3 17.5 1.0 CB B:CYS325 3.4 28.0 1.0 CB B:CYS334 3.5 24.0 1.0 CB B:HIS336 3.8 27.4 1.0 N B:CYS325 3.8 27.9 1.0 NE2 B:HIS336 4.0 26.0 1.0 CA B:CYS334 4.2 19.9 1.0 CA B:CYS325 4.2 20.1 1.0 CD2 B:HIS336 4.2 24.1 1.0 CD B:PRO335 4.3 30.2 1.0 N B:HIS336 4.4 24.5 1.0 CG2 B:VAL329 4.6 22.9 1.0 N B:PRO335 4.6 24.4 1.0 C B:CYS334 4.7 23.4 1.0 CA B:CYS322 4.7 24.9 1.0 CA B:HIS336 4.8 26.8 1.0 O B:HOH570 4.8 21.8 1.0 CB B:LYS324 4.9 24.5 1.0 C B:LYS324 4.9 26.5 1.0

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