Chlorine in PDB 2ies: Crystal Structure of Aquifex Aeolicus Lpxc Complexed with Pyrophosphate

The structure of Crystal Structure of Aquifex Aeolicus Lpxc Complexed with Pyrophosphate, PDB code: 2ies was solved by H.A.Gennadios, D.W.Christianson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 3.10
Space group	P 61
Cell size a, b, c (Å), α, β, γ (°)	98.850, 98.850, 125.660, 90.00, 90.00, 120.00
R / Rfree (%)	23 / 27.7

The structure of Crystal Structure of Aquifex Aeolicus Lpxc Complexed with Pyrophosphate also contains other interesting chemical elements:

Zinc

(Zn)

5 atoms

The binding sites of Chlorine atom in the Crystal Structure of Aquifex Aeolicus Lpxc Complexed with Pyrophosphate (pdb code 2ies). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structure of Aquifex Aeolicus Lpxc Complexed with Pyrophosphate, PDB code: 2ies:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Crystal Structure of Aquifex Aeolicus Lpxc Complexed with Pyrophosphate


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 Aquifex Aeolicus Lpxc Complexed with Pyrophosphate within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl607 b:30.0 occ:0.70 ZN A:ZN604 2.3 30.8 0.6

Chlorine binding site 2 out of 2 in the Crystal Structure of Aquifex Aeolicus Lpxc Complexed with Pyrophosphate


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of Aquifex Aeolicus Lpxc Complexed with Pyrophosphate within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl608 b:18.4 occ:0.70 ZN A:ZN602 2.3 26.8 0.6

H.A.Gennadios, D.W.Christianson. Binding of Uridine 5-Diphosphate in the Basic Patch of the Zinc Metalloenzyme Deacetylase Lpxc and Implications For Substrate Binding Biochemistry V. 45 15216 2006.
ISSN: ISSN 0006-2960
PubMed: 17176043
DOI: 10.1021/BI0619021