Chlorine in PDB 8a8h: Aps Kinase From Methanothermococcus Thermolithotrophicus Refined to 1.77 A

All present enzymatic activity of Aps Kinase From Methanothermococcus Thermolithotrophicus Refined to 1.77 A:
2.7.1.25;

The structure of Aps Kinase From Methanothermococcus Thermolithotrophicus Refined to 1.77 A, PDB code: 8a8h 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)	44.04 / 1.77
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	51.539, 176.176, 51.61, 90, 105.78, 90
R / Rfree (%)	15.4 / 18.1

The binding sites of Chlorine atom in the Aps Kinase From Methanothermococcus Thermolithotrophicus Refined to 1.77 A (pdb code 8a8h). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 4 binding sites of Chlorine where determined in the Aps Kinase From Methanothermococcus Thermolithotrophicus Refined to 1.77 A, PDB code: 8a8h:
Jump to Chlorine binding site number: 1; 2; 3; 4;

Chlorine binding site 1 out of 4 in the Aps Kinase From Methanothermococcus Thermolithotrophicus Refined to 1.77 A


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Aps Kinase From Methanothermococcus Thermolithotrophicus Refined to 1.77 A within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl307 b:81.9 occ:1.00 NZ A:LYS46 3.2 82.1 1.0 CD A:LYS46 3.9 53.7 1.0 CE A:LYS46 4.2 67.2 1.0 CE2 A:PHE48 4.3 38.4 1.0 CZ A:PHE48 4.3 33.2 1.0 NE2 A:GLN184 4.4 45.4 1.0 CG2 A:ILE180 4.5 35.0 1.0 CD1 A:LEU189 4.8 47.3 1.0 O A:HOH408 4.8 54.3 1.0 CB A:LEU189 4.9 40.0 1.0 CD A:GLN184 5.0 42.1 1.0

Chlorine binding site 2 out of 4 in the Aps Kinase From Methanothermococcus Thermolithotrophicus Refined to 1.77 A


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Aps Kinase From Methanothermococcus Thermolithotrophicus Refined to 1.77 A within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl205 b:88.5 occ:1.00 NZ B:LYS46 3.4 82.8 1.0 CD B:LYS46 3.5 64.0 1.0 CE B:LYS46 4.0 73.8 1.0 CE2 B:PHE48 4.2 40.2 1.0 CZ B:PHE48 4.4 39.5 1.0 CG2 B:ILE180 4.5 33.3 1.0 CG B:LYS46 4.8 48.8 1.0 NE2 B:GLN184 4.8 51.9 1.0

Chlorine binding site 3 out of 4 in the Aps Kinase From Methanothermococcus Thermolithotrophicus Refined to 1.77 A


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Aps Kinase From Methanothermococcus Thermolithotrophicus Refined to 1.77 A within 5.0Å range: probe atom residue distance (Å) B Occ C:Cl205 b:95.1 occ:1.00 NZ C:LYS46 2.9 87.2 1.0 CD C:LYS46 3.3 66.7 1.0 CE C:LYS46 3.5 70.5 1.0 CE2 C:PHE48 4.2 42.4 1.0 CZ C:PHE48 4.4 41.2 1.0 CG2 C:ILE180 4.7 31.9 1.0 NE2 C:GLN184 4.7 49.7 1.0 CG C:LYS46 4.7 49.9 1.0 NZ C:LYS14 4.8 98.0 1.0

Chlorine binding site 4 out of 4 in the Aps Kinase From Methanothermococcus Thermolithotrophicus Refined to 1.77 A


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Aps Kinase From Methanothermococcus Thermolithotrophicus Refined to 1.77 A within 5.0Å range: probe atom residue distance (Å) B Occ D:Cl207 b:85.4 occ:1.00 NZ D:LYS46 2.9 81.1 1.0 CD D:LYS46 3.4 70.8 1.0 CE D:LYS46 3.7 69.0 1.0 CE2 D:PHE48 3.9 44.0 1.0 CZ D:PHE48 4.0 47.7 1.0 NE2 D:GLN184 4.1 59.3 1.0 CG2 D:ILE180 4.7 41.6 1.0 CD1 D:LEU189 4.7 41.5 1.0 CG D:LYS46 4.9 46.3 1.0 OXT D:LEU189 5.0 58.8 1.0 CD D:GLN184 5.0 56.4 1.0

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