Chlorine in PDB 3qte: Crystal Structure of Human Alpha-Defensin 6 (H27W Mutant)

The structure of Crystal Structure of Human Alpha-Defensin 6 (H27W Mutant), PDB code: 3qte was solved by M.Pazgier, W.Lu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 1.95
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	33.774, 32.675, 54.005, 90.00, 108.35, 90.00
R / Rfree (%)	19.2 / 24.7

The binding sites of Chlorine atom in the Crystal Structure of Human Alpha-Defensin 6 (H27W Mutant) (pdb code 3qte). 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 6 (H27W Mutant), PDB code: 3qte:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Crystal Structure of Human Alpha-Defensin 6 (H27W 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 6 (H27W Mutant) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl33 b:74.3 occ:1.00 CZ A:PHE2 4.3 41.9 1.0 CE1 A:PHE2 4.4 42.6 1.0

Chlorine binding site 2 out of 2 in the Crystal Structure of Human Alpha-Defensin 6 (H27W 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 6 (H27W Mutant) within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl33 b:73.0 occ:1.00 SG B:CYS6 4.2 40.6 1.0 CG2 A:VAL22 4.2 31.1 1.0 CG2 B:VAL22 4.3 35.7 1.0 CB B:CYS6 4.7 37.4 1.0 SG A:CYS6 4.7 28.1 1.0 CZ C:PHE2 5.0 48.5 1.0

H.Chu, M.Pazgier, G.Jung, S.P.Nuccio, P.A.Castillo, M.F.De Jong, M.G.Winter, S.E.Winter, J.Wehkamp, B.Shen, N.H.Salzman, M.A.Underwood, R.M.Tsolis, G.M.Young, W.Lu, R.I.Lehrer, A.J.Baumler, C.L.Bevins. Human Alpha-Defensin 6 Promotes Mucosal Innate Immunity Through Self-Assembled Peptide Nanonets. Science V. 337 477 2012.
ISSN: ISSN 0036-8075
PubMed: 22722251
DOI: 10.1126/SCIENCE.1218831