Chlorine in PDB 5mr3: Crystal Structure of Red Abalone Egg Verl Repeat 2 with Linker in Complex with Sperm Lysin at 1.8 A Resolution

The structure of Crystal Structure of Red Abalone Egg Verl Repeat 2 with Linker in Complex with Sperm Lysin at 1.8 A Resolution, PDB code: 5mr3 was solved by K.Nishimura, I.Raj, H.Sadat Al-Hosseini, D.De Sanctis, L.Jovine, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.32 / 1.80
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	75.870, 87.860, 92.550, 90.00, 100.93, 90.00
R / Rfree (%)	20.1 / 22.7

The binding sites of Chlorine atom in the Crystal Structure of Red Abalone Egg Verl Repeat 2 with Linker in Complex with Sperm Lysin at 1.8 A Resolution (pdb code 5mr3). 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 Red Abalone Egg Verl Repeat 2 with Linker in Complex with Sperm Lysin at 1.8 A Resolution, PDB code: 5mr3:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Crystal Structure of Red Abalone Egg Verl Repeat 2 with Linker in Complex with Sperm Lysin at 1.8 A Resolution


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 Red Abalone Egg Verl Repeat 2 with Linker in Complex with Sperm Lysin at 1.8 A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl903 b:33.1 occ:0.85 H F:LEU236 2.2 34.5 1.0 H B:GLY247 2.6 38.3 1.0 HH B:TYR249 2.7 35.3 1.0 OH B:TYR249 2.8 29.4 1.0 HE3 B:TRP246 2.9 34.6 1.0 HB3 F:LYS235 3.0 33.4 1.0 N F:LEU236 3.1 28.7 1.0 HA F:LYS235 3.1 32.6 1.0 HB3 B:TRP246 3.1 33.9 1.0 HE2 F:LYS235 3.1 52.3 1.0 HB2 F:LEU236 3.2 37.3 1.0 N B:GLY247 3.3 31.9 1.0 O F:HOH548 3.3 29.4 1.0 CZ B:TYR249 3.4 29.3 1.0 HA2 B:GLY247 3.6 36.4 1.0 HE3 F:LYS235 3.6 52.3 1.0 HB3 F:LEU236 3.6 37.3 1.0 CA F:LYS235 3.7 27.1 1.0 HE1 B:TYR249 3.7 38.0 1.0 CB F:LYS235 3.7 27.9 1.0 HG2 F:LYS235 3.7 37.2 1.0 CE3 B:TRP246 3.7 28.8 1.0 CB F:LEU236 3.8 31.1 1.0 CE1 B:TYR249 3.8 31.7 1.0 CE F:LYS235 3.8 43.6 1.0 C F:LYS235 3.9 27.8 1.0 O B:HOH1029 3.9 29.4 0.9 CA B:GLY247 3.9 30.4 1.0 CA F:LEU236 4.0 31.5 1.0 CB B:TRP246 4.0 28.3 1.0 HA B:TRP246 4.1 31.8 1.0 CG F:LYS235 4.1 31.0 1.0 CE2 B:TYR249 4.2 28.3 1.0 C B:TRP246 4.2 24.8 1.0 CA B:TRP246 4.4 26.5 1.0 HE2 B:TYR249 4.4 33.9 1.0 O B:GLY247 4.4 27.9 1.0 C B:GLY247 4.5 28.0 1.0 H F:LEU237 4.5 35.9 1.0 CD2 B:TRP246 4.5 29.5 1.0 HB2 F:LYS235 4.5 33.4 1.0 HZ3 B:TRP246 4.5 34.1 1.0 CD F:LYS235 4.6 34.6 1.0 HA F:LEU236 4.6 37.8 1.0 CZ3 B:TRP246 4.6 28.4 1.0 HB2 B:TRP246 4.7 33.9 1.0 CG B:TRP246 4.7 29.3 1.0 HA3 B:GLY247 4.8 36.4 1.0 CD1 B:TYR249 4.8 33.1 1.0 HZ1 F:LYS235 4.8 60.5 1.0 NZ F:LYS235 4.9 50.5 1.0 O F:ASN234 5.0 27.3 1.0

Chlorine binding site 2 out of 2 in the Crystal Structure of Red Abalone Egg Verl Repeat 2 with Linker in Complex with Sperm Lysin at 1.8 A Resolution


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 Red Abalone Egg Verl Repeat 2 with Linker in Complex with Sperm Lysin at 1.8 A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ F:Cl401 b:36.9 occ:0.90 H B:LEU236 2.2 35.0 1.0 H F:GLY247 2.6 34.4 1.0 HH F:TYR249 2.7 40.8 1.0 HZ2 B:LYS235 2.8 60.2 1.0 HB3 B:LYS235 2.9 34.2 1.0 HE3 F:TRP246 2.9 39.0 1.0 OH F:TYR249 2.9 34.0 1.0 HA B:LYS235 3.0 33.6 1.0 N B:LEU236 3.0 29.2 1.0 HB3 F:TRP246 3.2 33.6 1.0 N F:GLY247 3.3 28.6 1.0 HB2 B:LEU236 3.3 47.2 1.0 O B:HOH1055 3.4 29.4 1.0 CZ F:TYR249 3.4 33.9 1.0 HG2 B:LYS235 3.5 41.3 1.0 HE1 F:TYR249 3.5 42.2 1.0 NZ B:LYS235 3.5 50.2 1.0 HA2 F:GLY247 3.5 34.0 1.0 HZ1 B:LYS235 3.5 60.2 1.0 CB B:LYS235 3.5 28.5 1.0 CA B:LYS235 3.6 28.0 1.0 HE3 B:LYS235 3.6 54.8 1.0 CE1 F:TYR249 3.6 35.1 1.0 HB3 B:LEU236 3.7 47.2 1.0 CE3 F:TRP246 3.7 32.5 1.0 C B:LYS235 3.8 28.3 1.0 CB B:LEU236 3.8 39.3 1.0 O F:HOH511 3.8 29.5 0.9 CA F:GLY247 3.9 28.3 1.0 CG B:LYS235 4.0 34.5 1.0 CA B:LEU236 4.0 29.7 1.0 CE B:LYS235 4.1 45.7 1.0 CB F:TRP246 4.1 28.0 1.0 HA F:TRP246 4.1 34.8 1.0 HZ3 B:LYS235 4.2 60.2 1.0 O F:GLY247 4.2 32.7 1.0 C F:TRP246 4.3 29.3 1.0 CE2 F:TYR249 4.3 30.4 1.0 HB2 B:LYS235 4.4 34.2 1.0 CA F:TRP246 4.4 29.0 1.0 C F:GLY247 4.4 29.9 1.0 HZ3 F:TRP246 4.5 41.7 1.0 H B:LEU237 4.5 36.0 1.0 CD2 F:TRP246 4.5 29.2 1.0 HE2 F:TYR249 4.5 36.4 1.0 HA B:LEU236 4.6 35.6 1.0 CZ3 F:TRP246 4.6 34.8 1.0 CD B:LYS235 4.7 38.4 1.0 CD1 F:TYR249 4.7 32.2 1.0 HB2 F:TRP246 4.7 33.6 1.0 CG F:TRP246 4.7 28.6 1.0 HA3 F:GLY247 4.7 34.0 1.0 HG3 B:LYS235 4.8 41.3 1.0 HE2 B:LYS235 4.9 54.8 1.0 N B:LYS235 4.9 27.1 1.0 O B:ASN234 4.9 27.2 1.0

I.Raj, H.Sadat Al Hosseini, E.Dioguardi, K.Nishimura, L.Han, A.Villa, D.De Sanctis, L.Jovine. Structural Basis of Egg Coat-Sperm Recognition at Fertilization. Cell V. 169 1315 2017.
ISSN: ISSN 1097-4172
PubMed: 28622512
DOI: 10.1016/J.CELL.2017.05.033