Zinc in PDB 8a8g: Atp Sulfurylase From Methanothermococcus Thermolithotrophicus - Orthorhombic Form

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

The structure of Atp Sulfurylase From Methanothermococcus Thermolithotrophicus - Orthorhombic Form, PDB code: 8a8g 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)	49.73 / 1.97
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	55.705, 154.457, 157.575, 90, 90, 90
R / Rfree (%)	18.9 / 21.8

The binding sites of Zinc atom in the Atp Sulfurylase From Methanothermococcus Thermolithotrophicus - Orthorhombic Form (pdb code 8a8g). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Atp Sulfurylase From Methanothermococcus Thermolithotrophicus - Orthorhombic Form, PDB code: 8a8g:

Zinc binding site 1 out of 1 in the Atp Sulfurylase From Methanothermococcus Thermolithotrophicus - Orthorhombic 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 - Orthorhombic Form within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn407 b:23.6 occ:1.00 ND1 A:HIS336 2.1 29.5 1.0 SG A:CYS325 2.3 26.3 1.0 SG A:CYS334 2.3 39.1 1.0 SG A:CYS322 2.3 33.8 1.0 CE1 A:HIS336 2.9 30.1 1.0 CG A:HIS336 3.2 25.0 1.0 CB A:CYS322 3.3 26.2 1.0 CB A:CYS325 3.3 25.0 1.0 CB A:CYS334 3.4 37.1 1.0 N A:CYS325 3.7 27.5 1.0 CB A:HIS336 3.7 26.1 1.0 NE2 A:HIS336 4.1 26.7 1.0 CA A:CYS325 4.1 24.1 1.0 CA A:CYS334 4.2 29.3 1.0 CD2 A:HIS336 4.3 25.6 1.0 CD A:PRO335 4.5 31.3 1.0 N A:HIS336 4.5 35.9 1.0 CG2 A:VAL329 4.6 28.4 1.0 CA A:CYS322 4.7 29.6 1.0 C A:CYS334 4.7 33.0 1.0 N A:PRO335 4.7 32.5 1.0 C A:LYS324 4.7 26.5 1.0 CA A:HIS336 4.8 30.2 1.0 CB A:LYS324 4.9 24.1 1.0

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