Chlorine in PDB 1yik: Structure of Hen Egg White Lysozyme Soaked with Cu-Cyclam

All present enzymatic activity of Structure of Hen Egg White Lysozyme Soaked with Cu-Cyclam:
3.2.1.17;

The structure of Structure of Hen Egg White Lysozyme Soaked with Cu-Cyclam, PDB code: 1yik was solved by T.M.Hunter, I.W.Mcnae, X.Liang, J.Bella, S.Parsons, M.D.Walkinshaw, P.J.Sadler, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	55.00 / 1.75
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	77.906, 77.906, 37.762, 90.00, 90.00, 90.00
R / Rfree (%)	17.6 / 23.3

The structure of Structure of Hen Egg White Lysozyme Soaked with Cu-Cyclam also contains other interesting chemical elements:

Copper	(Cu)	2 atoms
Sodium	(Na)	1 atom

The binding sites of Chlorine atom in the Structure of Hen Egg White Lysozyme Soaked with Cu-Cyclam (pdb code 1yik). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Structure of Hen Egg White Lysozyme Soaked with Cu-Cyclam, PDB code: 1yik:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Structure of Hen Egg White Lysozyme Soaked with Cu-Cyclam


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structure of Hen Egg White Lysozyme Soaked with Cu-Cyclam within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl502 b:30.7 occ:1.00 OH A:TYR23 2.8 14.3 1.0 O A:HOH533 3.5 21.6 1.0 CZ A:TYR23 3.5 12.0 1.0 CE2 A:TYR23 3.6 13.4 1.0 CA A:GLY104 4.2 14.3 1.0 O A:ARG21 4.6 17.1 1.0 CE1 A:TYR23 4.7 11.3 1.0 CD2 A:TYR23 4.8 10.9 1.0 N A:GLY104 4.9 14.5 1.0 O A:HOH544 5.0 29.6 1.0

Chlorine binding site 2 out of 2 in the Structure of Hen Egg White Lysozyme Soaked with Cu-Cyclam


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Structure of Hen Egg White Lysozyme Soaked with Cu-Cyclam within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl503 b:33.0 occ:1.00 O A:HOH527 2.9 14.8 1.0 N A:THR69 3.0 17.5 1.0 O A:THR69 3.2 19.3 1.0 N A:ARG68 3.4 18.1 1.0 N A:GLY67 3.4 16.6 1.0 ND2 A:ASN65 3.4 19.1 1.0 C A:GLY67 3.5 19.0 1.0 C A:THR69 3.5 20.1 1.0 CA A:GLY67 3.5 17.4 1.0 CA A:THR69 3.6 18.4 1.0 OG A:SER72 3.6 25.5 1.0 O A:HOH644 3.7 42.6 1.0 CB A:THR69 3.9 17.0 1.0 C A:ARG68 4.0 19.0 1.0 O A:HOH528 4.0 18.5 1.0 OD1 A:ASP66 4.1 15.8 1.0 CA A:ARG68 4.1 18.3 1.0 O A:GLY67 4.2 19.0 1.0 N A:PRO70 4.3 22.3 1.0 NA A:NA504 4.5 22.5 1.0 C A:ASP66 4.5 14.7 1.0 N A:ASP66 4.6 13.6 1.0 OG1 A:THR69 4.6 14.5 1.0 CG A:ASN65 4.7 16.9 1.0 CA A:PRO70 4.8 24.2 1.0 CB A:SER72 4.9 26.9 1.0

T.M.Hunter, I.W.Mcnae, X.Liang, J.Bella, S.Parsons, M.D.Walkinshaw, P.J.Sadler. Protein Recognition of Macrocycles: Binding of Anti-Hiv Metallocyclams to Lysozyme Proc.Natl.Acad.Sci.Usa V. 102 2288 2005.
ISSN: ISSN 0027-8424
PubMed: 15701702
DOI: 10.1073/PNAS.0407595102