Chlorine in PDB 2eht: Crystal Structure of Acyl Carrier Protein From Aquifex Aeolicus (Form 2)

The structure of Crystal Structure of Acyl Carrier Protein From Aquifex Aeolicus (Form 2), PDB code: 2eht was solved by H.Mizutani, N.Kunishima, Riken Structural Genomics/Proteomicsinitiative (Rsgi), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 1.40
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	30.312, 37.042, 61.104, 90.00, 90.00, 90.00
R / Rfree (%)	19.6 / 22.5

The structure of Crystal Structure of Acyl Carrier Protein From Aquifex Aeolicus (Form 2) also contains other interesting chemical elements:

Zinc

(Zn)

7 atoms

The binding sites of Chlorine atom in the Crystal Structure of Acyl Carrier Protein From Aquifex Aeolicus (Form 2) (pdb code 2eht). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Crystal Structure of Acyl Carrier Protein From Aquifex Aeolicus (Form 2), PDB code: 2eht:

Chlorine binding site 1 out of 1 in the Crystal Structure of Acyl Carrier Protein From Aquifex Aeolicus (Form 2)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Acyl Carrier Protein From Aquifex Aeolicus (Form 2) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl208 b:8.2 occ:1.00 N A:GLY77 3.2 11.9 1.0 CA A:GLY77 3.4 12.5 1.0 C A:GLY77 3.5 13.2 1.0 O A:HOH226 3.7 12.8 1.0 CG2 A:VAL75 3.7 10.3 1.0 NH1 A:ARG5 3.7 7.5 1.0 O A:GLY77 3.8 14.4 1.0 OXT A:GLY77 3.9 12.8 1.0 CB A:VAL75 3.9 10.7 1.0 CD1 A:PHE49 4.1 9.0 1.0 CE1 A:PHE49 4.1 9.1 1.0 CD1 A:LEU2 4.4 15.1 1.0 C A:GLY76 4.5 11.4 1.0 N A:GLY76 4.5 11.4 1.0 O A:HOH255 4.7 10.6 1.0 CG1 A:VAL75 4.8 12.4 1.0 CZ A:ARG5 4.9 7.3 1.0 C A:VAL75 5.0 11.2 1.0 CG A:LEU2 5.0 12.9 1.0 CA A:GLY76 5.0 11.6 1.0

H.Mizutani, N.Kunishima. Crystal Structure of Acyl Carrier Protein From Aquifex Aeolicus To Be Published.