Chlorine in PDB 4du0: Crystal Structure of Human Alpha-Defensin 1, HNP1 (G17A Mutant)

The structure of Crystal Structure of Human Alpha-Defensin 1, HNP1 (G17A Mutant), PDB code: 4du0 was solved by X.Wu, W.Lu, M.Pazgier, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	42.28 / 1.90
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	38.453, 50.083, 78.883, 90.00, 90.00, 90.00
R / Rfree (%)	17.5 / 21.2

The binding sites of Chlorine atom in the Crystal Structure of Human Alpha-Defensin 1, HNP1 (G17A Mutant) (pdb code 4du0). 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 Human Alpha-Defensin 1, HNP1 (G17A Mutant), PDB code: 4du0:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Crystal Structure of Human Alpha-Defensin 1, HNP1 (G17A Mutant)


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 Human Alpha-Defensin 1, HNP1 (G17A Mutant) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl102 b:65.7 occ:1.00 O A:HOH223 2.4 52.3 1.0 O A:LEU25 3.5 20.5 1.0 O A:PRO7 3.7 35.2 1.0 N A:ALA27 4.0 22.4 1.0 O A:HOH209 4.0 41.7 1.0 C A:LEU25 4.2 20.0 1.0 CA A:TRP26 4.3 21.2 1.0 NH1 A:ARG15 4.3 29.1 1.0 C A:TRP26 4.3 21.4 1.0 C A:PRO7 4.5 34.4 1.0 O A:ARG5 4.5 25.3 1.0 N A:TRP26 4.5 19.1 1.0 NH2 A:ARG15 4.7 30.3 1.0 CA A:PRO7 4.8 34.2 1.0 CG1 A:ILE6 4.8 26.5 1.0 CZ A:ARG15 4.8 33.4 1.0 CA A:ALA27 4.8 21.8 1.0 CB A:LEU25 4.8 19.3 1.0 CB A:ALA27 4.9 22.2 1.0

Chlorine binding site 2 out of 2 in the Crystal Structure of Human Alpha-Defensin 1, HNP1 (G17A Mutant)


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 Human Alpha-Defensin 1, HNP1 (G17A Mutant) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl103 b:32.2 occ:1.00 N A:ALA1 3.1 22.5 1.0 NH2 B:ARG15 3.2 25.9 1.0 O A:ALA1 3.6 22.6 1.0 CD1 B:LEU25 4.0 28.8 1.0 CA A:ALA1 4.0 21.4 1.0 CB B:LEU25 4.0 18.6 1.0 CB A:ALA1 4.0 21.4 1.0 CZ B:ARG15 4.2 24.8 1.0 NH1 B:ARG15 4.2 26.5 1.0 C A:ALA1 4.2 21.7 1.0 CG2 B:THR18 4.3 18.5 1.0 CE2 A:TYR3 4.7 28.5 1.0 CG B:LEU25 4.7 25.1 1.0 O B:HOH205 4.8 29.0 1.0 OG1 B:THR18 4.9 21.7 1.0 OH A:TYR3 4.9 31.0 1.0

L.Zhao, B.Ericksen, X.Wu, C.Zhan, W.Yuan, X.Li, M.Pazgier, W.Lu. Invariant Gly Residue Is Important For Alpha-Defensin Folding, Dimerization, and Function: A Case Study of the Human Neutrophil Alpha-Defensin HNP1 J.Biol.Chem. V. 287 18900 2012.
ISSN: ISSN 0021-9258
PubMed: 22496447
DOI: 10.1074/JBC.M112.355255