Chlorine in PDB 4hqf: Crystal Structure of Plasmodium Falciparum Trap, I4 Form

The structure of Crystal Structure of Plasmodium Falciparum Trap, I4 Form, PDB code: 4hqf was solved by G.Song, A.C.Koksal, C.Lu, T.A.Springer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	34.85 / 2.20
Space group	I 4
Cell size a, b, c (Å), α, β, γ (°)	110.220, 110.220, 47.050, 90.00, 90.00, 90.00
R / Rfree (%)	17.3 / 21.7

The binding sites of Chlorine atom in the Crystal Structure of Plasmodium Falciparum Trap, I4 Form (pdb code 4hqf). 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 Crystal Structure of Plasmodium Falciparum Trap, I4 Form, PDB code: 4hqf:

Chlorine binding site 1 out of 1 in the Crystal Structure of Plasmodium Falciparum Trap, I4 Form


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 Plasmodium Falciparum Trap, I4 Form within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl401 b:50.7 occ:1.00 O A:HOH605 2.8 53.4 1.0 OG1 A:THR134 3.2 53.3 1.0 O A:HOH522 3.2 50.8 1.0 OG A:SER132 3.3 50.8 1.0 N A:SER167 3.4 52.3 1.0 N A:ASP166 3.4 53.5 1.0 CB A:ASP166 3.6 84.9 1.0 N A:THR134 3.6 28.5 1.0 N A:LEU133 3.6 36.6 1.0 CB A:THR134 3.8 45.1 1.0 CB A:PRO165 3.9 41.4 1.0 CA A:ASP166 3.9 62.0 1.0 OG A:SER171 4.0 61.7 1.0 CA A:SER132 4.0 38.1 1.0 CB A:SER132 4.0 44.6 1.0 O A:SER167 4.1 42.4 1.0 C A:ASP166 4.1 55.2 1.0 C A:SER132 4.1 40.9 1.0 C A:PRO165 4.2 50.6 1.0 CA A:PRO165 4.3 41.2 1.0 CA A:THR134 4.3 46.2 1.0 CA A:SER167 4.3 52.0 1.0 CA A:LEU133 4.4 32.3 1.0 CB A:SER167 4.5 49.6 1.0 C A:LEU133 4.5 30.3 1.0 CB A:LEU133 4.5 32.8 1.0 C A:SER167 4.6 42.3 1.0 CG A:ASP166 4.7 0.3 1.0 OD2 A:ASP166 4.9 1.0 1.0 O A:HOH583 4.9 58.2 1.0

G.Song, A.C.Koksal, C.Lu, T.A.Springer. Shape Change in the Receptor For Gliding Motility in Plasmodium Sporozoites. Proc.Natl.Acad.Sci.Usa V. 109 21420 2012.
ISSN: ISSN 0027-8424
PubMed: 23236185
DOI: 10.1073/PNAS.1218581109