Chlorine in PDB 9fqb: Crystal Structure of CLY21-HNP1

The structure of Crystal Structure of CLY21-HNP1, PDB code: 9fqb was solved by S.Becker, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	31.49 / 1.09
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	46.075, 46.075, 51.282, 90, 90, 120
R / Rfree (%)	11.1 / 12.2

The binding sites of Chlorine atom in the Crystal Structure of CLY21-HNP1 (pdb code 9fqb). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the Crystal Structure of CLY21-HNP1, PDB code: 9fqb:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in the Crystal Structure of CLY21-HNP1


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 CLY21-HNP1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl21 b:15.2 occ:0.28 CL A:3CT21 0.0 15.2 0.3 CE2 A:3CT21 1.7 14.2 0.3 CL A:3CT21 1.8 17.1 0.4 HH A:3CT21 2.6 16.4 0.3 CZ A:3CT21 2.7 13.5 0.3 CD2 A:3CT21 2.7 13.7 0.3 HD2 A:3CT21 2.8 16.4 0.3 OH A:3CT21 2.9 13.7 0.3 HD2 A:3CT21 2.9 17.8 0.7 CE2 A:3CT21 3.0 16.8 0.7 CD2 A:3CT21 3.3 14.8 0.7 HH2 A:TRP26 3.4 14.6 1.0 CH2 A:TRP26 3.6 12.1 1.0 CE1 A:3CT21 4.0 12.9 0.3 CG A:3CT21 4.0 13.0 0.3 CZ2 A:TRP26 4.1 11.3 1.0 HZ2 A:TRP26 4.1 13.6 1.0 CZ3 A:TRP26 4.2 12.0 1.0 HD2 B:TYR16 4.2 16.3 1.0 CZ A:3CT21 4.3 17.3 0.7 HZ3 A:TRP26 4.3 14.4 1.0 HG3 A:GLN22 4.4 30.7 1.0 O A:HOH201 4.4 36.0 0.8 CD1 A:3CT21 4.5 12.6 0.3 HE1 A:3CT21 4.7 15.5 0.3 CG A:3CT21 4.7 13.8 0.7 OH A:3CT21 4.8 19.1 0.7 CE2 A:TRP26 4.9 10.3 1.0

Chlorine binding site 2 out of 3 in the Crystal Structure of CLY21-HNP1


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 CLY21-HNP1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl21 b:17.1 occ:0.44 CL A:3CT21 0.0 17.1 0.4 CE2 A:3CT21 1.5 14.2 0.3 CZ A:3CT21 1.5 13.5 0.3 OH A:3CT21 1.7 13.7 0.3 CE2 A:3CT21 1.7 16.8 0.7 CL A:3CT21 1.8 15.2 0.3 HH A:3CT21 1.9 16.4 0.3 CD2 A:3CT21 2.7 14.8 0.7 CD2 A:3CT21 2.7 13.7 0.3 HD2 A:3CT21 2.7 17.8 0.7 CE1 A:3CT21 2.8 12.9 0.3 CZ A:3CT21 2.8 17.3 0.7 HG3 A:GLN22 3.0 30.7 1.0 OH A:3CT21 3.1 19.1 0.7 O A:HOH201 3.2 36.0 0.8 HD2 A:3CT21 3.3 16.4 0.3 HE1 A:3CT21 3.3 15.5 0.3 CD1 A:3CT21 3.6 12.6 0.3 CG A:3CT21 3.6 13.0 0.3 HD2 B:TYR16 3.8 16.3 1.0 CG A:GLN22 3.9 25.5 1.0 CD A:GLN22 3.9 28.4 1.0 CG A:3CT21 4.0 13.8 0.7 CE1 A:3CT21 4.1 15.8 0.7 NE2 A:GLN22 4.1 30.3 1.0 HE21 A:GLN22 4.1 36.4 1.0 HG2 A:GLN22 4.4 30.7 1.0 OE1 A:GLN22 4.4 30.4 1.0 HD1 A:3CT21 4.5 15.1 0.3 HE22 A:GLN22 4.5 36.4 1.0 HH2 A:TRP26 4.5 14.6 1.0 HZ2 A:TRP26 4.5 13.6 1.0 CD1 A:3CT21 4.5 14.7 0.7 HE2 B:TYR16 4.6 17.6 1.0 CD2 B:TYR16 4.6 13.6 1.0 HB2 A:GLN22 4.6 25.4 1.0 HE1 A:3CT21 4.8 19.0 0.7 CH2 A:TRP26 4.8 12.1 1.0 CZ2 A:TRP26 4.8 11.3 1.0 CB A:GLN22 4.9 21.2 1.0

Chlorine binding site 3 out of 3 in the Crystal Structure of CLY21-HNP1


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Crystal Structure of CLY21-HNP1 within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl21 b:13.4 occ:0.97 CL B:3CT21 0.0 13.4 1.0 CE2 B:3CT21 1.7 10.7 1.0 CZ B:3CT21 2.7 10.6 1.0 CD2 B:3CT21 2.7 10.7 1.0 HD2 B:3CT21 2.8 12.8 1.0 OH B:3CT21 3.0 11.1 1.0 CH2 B:TRP26 3.6 11.6 1.0 HH2 B:TRP26 3.6 13.9 1.0 HB2 B:CYS4 3.8 10.8 1.0 CZ2 B:TRP26 3.8 11.4 1.0 CE1 B:3CT21 4.0 10.8 1.0 HZ2 B:TRP26 4.0 13.8 1.0 CG B:3CT21 4.0 10.3 1.0 CZ3 B:TRP26 4.1 11.8 1.0 HE22 B:GLN22 4.1 15.6 1.0 HZ3 B:TRP26 4.3 14.2 1.0 NE2 B:GLN22 4.3 13.0 1.0 HB2 B:GLN22 4.4 14.6 1.0 CE2 B:TRP26 4.4 10.0 1.0 CD1 B:3CT21 4.5 11.1 1.0 HE21 B:GLN22 4.6 15.6 1.0 OE1 B:GLN22 4.6 12.7 1.0 CE3 B:TRP26 4.6 10.1 1.0 O B:HOH219 4.7 9.8 1.0 HE1 B:3CT21 4.7 13.0 1.0 CD B:GLN22 4.7 12.2 1.0 CB B:CYS4 4.7 9.0 1.0 CD2 B:TRP26 4.8 9.7 1.0 HE2 A:PHE28 4.9 13.4 1.0 HB3 B:GLN22 4.9 14.6 1.0 HZ A:PHE28 5.0 12.3 1.0 HB3 B:CYS4 5.0 10.8 1.0

S.Becker, S.Becker. N/A N/A.