Chlorine in PDB 7lcv: Factor H Enhancing Human Antibody Fragment (Fab) to Meningococcal Factor H Binding Protein

The structure of Factor H Enhancing Human Antibody Fragment (Fab) to Meningococcal Factor H Binding Protein, PDB code: 7lcv was solved by P.T.Beernink, N.Sands, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	81.18 / 1.70
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	39.47, 52.37, 84.56, 73.78, 84.48, 74.17
R / Rfree (%)	24 / 27

The binding sites of Chlorine atom in the Factor H Enhancing Human Antibody Fragment (Fab) to Meningococcal Factor H Binding Protein (pdb code 7lcv). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Factor H Enhancing Human Antibody Fragment (Fab) to Meningococcal Factor H Binding Protein, PDB code: 7lcv:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Factor H Enhancing Human Antibody Fragment (Fab) to Meningococcal Factor H Binding Protein


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Factor H Enhancing Human Antibody Fragment (Fab) to Meningococcal Factor H Binding Protein within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl301 b:52.0 occ:1.00 O B:HOH472 3.6 40.2 1.0 O B:HOH469 3.6 53.3 1.0 HB3 B:SER158 3.7 64.5 1.0 O B:HOH410 4.0 49.6 1.0 H B:SER158 4.1 52.0 1.0 CB B:SER158 4.6 53.7 1.0 HA B:GLN157 4.6 49.8 1.0 N B:SER158 4.6 43.2 1.0 O B:HOH494 4.6 42.7 1.0 O B:LEU156 4.7 47.4 1.0 HB2 B:SER158 4.7 64.5 1.0 O B:SER158 4.8 41.3 1.0

Chlorine binding site 2 out of 2 in the Factor H Enhancing Human Antibody Fragment (Fab) to Meningococcal Factor H Binding Protein


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Factor H Enhancing Human Antibody Fragment (Fab) to Meningococcal Factor H Binding Protein within 5.0Å range: probe atom residue distance (Å) B Occ C:Cl301 b:41.8 occ:1.00 O C:HOH505 2.7 50.4 1.0 HD2 C:LYS55 3.0 65.1 1.0 O C:LEU48 3.4 36.8 1.0 HA C:ALA49 3.4 46.5 1.0 HD2 C:PHE76 3.5 37.1 1.0 H C:LYS55 3.5 50.2 1.0 HA C:GLU54 3.5 45.8 1.0 H C:ALA50 3.5 39.6 1.0 HB2 C:LYS55 3.5 46.2 1.0 HE2 C:PHE76 3.6 46.6 1.0 HB3 C:ALA53 3.6 54.5 1.0 HB1 C:ALA53 3.6 54.5 1.0 HB2 C:LEU48 3.6 39.8 1.0 HG3 C:LYS55 3.7 55.8 1.0 O C:ALA53 3.8 38.0 1.0 C C:LEU48 3.8 33.0 1.0 HB3 C:ALA50 3.9 43.8 1.0 N C:ALA50 3.9 32.9 1.0 N C:LYS55 3.9 41.7 1.0 CD C:LYS55 3.9 54.2 1.0 C C:ALA53 3.9 39.8 1.0 HB3 C:LEU48 4.0 39.8 1.0 CB C:ALA53 4.0 45.3 1.0 CA C:ALA49 4.0 38.6 1.0 CA C:GLU54 4.1 38.0 1.0 CG C:LYS55 4.1 46.4 1.0 N C:GLU54 4.1 37.7 1.0 CD2 C:PHE76 4.1 30.8 1.0 C C:ALA49 4.1 29.9 1.0 CE2 C:PHE76 4.2 38.7 1.0 N C:ALA49 4.2 32.4 1.0 CB C:LYS55 4.2 38.4 1.0 CB C:LEU48 4.2 33.1 1.0 C C:GLU54 4.3 40.0 1.0 HE3 C:LYS55 4.4 77.9 1.0 HB2 C:ALA50 4.5 43.8 1.0 HD3 C:LYS55 4.5 65.1 1.0 CB C:ALA50 4.5 36.4 1.0 H C:GLU54 4.6 45.4 1.0 CA C:ALA53 4.6 41.8 1.0 CA C:LYS55 4.7 39.4 1.0 CA C:LEU48 4.7 27.4 1.0 CE C:LYS55 4.7 64.8 1.0 CA C:ALA50 4.8 32.9 1.0 H C:ALA49 4.8 39.0 1.0 HB2 C:ALA53 4.9 54.5 1.0 O C:ALA50 4.9 40.5 1.0 O C:ALA49 4.9 35.8 1.0 HZ2 C:LYS55 5.0 73.3 1.0 HE1 C:TYR57 5.0 47.2 1.0

N.Sands, P.T.Beernink. Structural Mechanisms For Enhancement of A Complement Regulator By Vaccine-Elicited Human Antibodies To Be Published.