Chlorine in PDB 9bni: X-Ray Crystal Structure of Cu-TZ4H-H3AH10D Tryptophan Zipper Metallo- Beta-Sheet Peptide

The structure of X-Ray Crystal Structure of Cu-TZ4H-H3AH10D Tryptophan Zipper Metallo- Beta-Sheet Peptide, PDB code: 9bni was solved by V.T.Dang, A.Nguyen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	22.76 / 1.20
Space group	I 21 3
Cell size a, b, c (Å), α, β, γ (°)	45.518, 45.518, 45.518, 90, 90, 90
R / Rfree (%)	17 / 21

The structure of X-Ray Crystal Structure of Cu-TZ4H-H3AH10D Tryptophan Zipper Metallo- Beta-Sheet Peptide also contains other interesting chemical elements:

Copper

(Cu)

1 atom

The binding sites of Chlorine atom in the X-Ray Crystal Structure of Cu-TZ4H-H3AH10D Tryptophan Zipper Metallo- Beta-Sheet Peptide (pdb code 9bni). 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 X-Ray Crystal Structure of Cu-TZ4H-H3AH10D Tryptophan Zipper Metallo- Beta-Sheet Peptide, PDB code: 9bni:

Chlorine binding site 1 out of 1 in the X-Ray Crystal Structure of Cu-TZ4H-H3AH10D Tryptophan Zipper Metallo- Beta-Sheet Peptide


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of X-Ray Crystal Structure of Cu-TZ4H-H3AH10D Tryptophan Zipper Metallo- Beta-Sheet Peptide within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl102 b:31.9 occ:0.33 HD1 A:TRP9 2.6 18.8 1.0 HA A:LYS8 3.1 19.2 1.0 O A:GLY7 3.2 16.1 1.0 H A:TRP9 3.3 17.9 1.0 CD1 A:TRP9 3.5 15.7 1.0 HB2 A:TRP9 3.8 19.4 1.0 N A:TRP9 3.9 14.9 1.0 CA A:LYS8 4.0 16.0 1.0 C A:GLY7 4.3 15.2 1.0 CG A:TRP9 4.3 15.2 1.0 C A:LYS8 4.4 16.0 1.0 CB A:TRP9 4.4 16.1 1.0 NE1 A:TRP9 4.5 15.2 1.0 HE1 A:TRP9 4.5 18.2 1.0 N A:LYS8 4.6 15.7 1.0 CA A:TRP9 4.8 16.6 1.0 HD1 A:TRP4 4.9 17.5 0.7

V.T.Dang, A.Engineer, D.Mcelheny, A.Drena, J.Telser, K.Tomczak, A.I.Nguyen. Crystallography Reveals Metal-Triggered Restructuring of Beta-Hairpins. Chemistry 02101 2024.
ISSN: ISSN 0947-6539
PubMed: 39152095
DOI: 10.1002/CHEM.202402101