Chlorine in PDB 7o4p: Cystal Structure of Zymogen Granule Protein 16 (ZG16)

The structure of Cystal Structure of Zymogen Granule Protein 16 (ZG16), PDB code: 7o4p was solved by G.Javitt, D.Fass, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	43.10 / 1.08
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	58.336, 58.336, 82.618, 90, 90, 120
R / Rfree (%)	16.5 / 17.5

The binding sites of Chlorine atom in the Cystal Structure of Zymogen Granule Protein 16 (ZG16) (pdb code 7o4p). 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 Cystal Structure of Zymogen Granule Protein 16 (ZG16), PDB code: 7o4p:

Chlorine binding site 1 out of 1 in the Cystal Structure of Zymogen Granule Protein 16 (ZG16)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Cystal Structure of Zymogen Granule Protein 16 (ZG16) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl202 b:16.4 occ:1.00 H A:TRP103 2.5 16.9 1.0 HZ1 A:LYS106 2.7 16.2 0.6 HB3 A:LYS102 2.7 17.0 1.0 H A:TYR104 2.8 15.1 1.0 HE1 A:TYR60 2.8 18.0 1.0 O A:HOH448 3.0 19.4 0.2 HD2 A:TYR104 3.0 18.9 1.0 HD2 A:LYS106 3.0 16.7 0.4 HD2 A:LYS106 3.1 17.0 0.6 O A:HOH324 3.1 21.7 1.0 N A:TRP103 3.2 14.1 1.0 HE3 A:TRP103 3.2 32.9 1.0 O A:HOH448 3.3 24.5 0.8 HB2 A:TRP103 3.3 19.9 1.0 NZ A:LYS106 3.5 13.5 0.6 N A:TYR104 3.5 12.6 1.0 HZ3 A:LYS106 3.7 16.2 0.6 CB A:LYS102 3.7 14.2 1.0 CE1 A:TYR60 3.7 15.0 1.0 HZ1 A:LYS106 3.9 17.9 0.4 CD2 A:TYR104 3.9 15.8 1.0 H A:LYS102 3.9 14.7 1.0 CD A:LYS106 3.9 14.2 0.6 HB2 A:TYR104 3.9 15.3 1.0 CD A:LYS106 3.9 13.9 0.4 HG2 A:LYS106 4.0 16.2 0.6 CA A:TRP103 4.0 15.2 1.0 CE3 A:TRP103 4.0 27.4 1.0 CB A:TRP103 4.0 16.6 1.0 HG2 A:LYS106 4.1 16.5 0.4 HB2 A:LYS102 4.1 17.0 1.0 HG3 A:LYS106 4.1 16.5 0.4 HZ2 A:LYS106 4.1 16.2 0.6 HH A:TYR60 4.1 21.8 1.0 HD1 A:TYR60 4.1 16.6 1.0 C A:TRP103 4.2 13.9 1.0 O A:TYR104 4.2 12.7 1.0 CE A:LYS106 4.2 14.8 0.6 C A:LYS102 4.2 13.1 1.0 HG3 A:LYS106 4.2 16.2 0.6 CA A:LYS102 4.2 13.1 1.0 CG A:LYS106 4.3 13.5 0.6 CG A:LYS106 4.3 13.8 0.4 N A:LYS102 4.3 12.3 1.0 HD3 A:LYS102 4.4 26.0 1.0 O A:HOH513 4.4 54.1 1.0 CD1 A:TYR60 4.4 13.8 1.0 HE2 A:LYS106 4.4 17.7 0.6 CA A:TYR104 4.4 11.6 1.0 HD3 A:LYS106 4.5 16.7 0.4 CB A:TYR104 4.5 12.8 1.0 HG2 A:LYS102 4.5 21.3 1.0 NZ A:LYS106 4.5 14.9 0.4 HE2 A:TYR104 4.6 21.0 1.0 CG A:LYS102 4.6 17.7 1.0 CD2 A:TRP103 4.6 22.9 1.0 HZ3 A:LYS106 4.6 17.9 0.4 CG A:TYR104 4.6 13.1 1.0 HD3 A:LYS106 4.7 17.0 0.6 CE2 A:TYR104 4.7 17.5 1.0 CG A:TRP103 4.7 19.0 1.0 C A:TYR104 4.7 11.9 1.0 CE A:LYS106 4.7 15.2 0.4 CZ A:TYR60 4.8 15.4 1.0 HB3 A:TRP103 4.8 19.9 1.0 OH A:TYR60 4.8 18.2 1.0 HA A:TRP103 4.9 18.2 1.0 HZ3 A:TRP103 4.9 49.6 1.0 CZ3 A:TRP103 4.9 41.4 1.0 HE2 A:LYS106 4.9 18.2 0.4 CD A:LYS102 5.0 21.6 1.0

G.Javitt, A.Kinzel, N.Reznik, D.Fass. Conformational Switches and Redox Properties of the Colon Cancer-Associated Human Lectin ZG16. Febs J. 2021.
ISSN: ISSN 1742-464X
PubMed: 34077620
DOI: 10.1111/FEBS.16044