Chlorine in PDB 7qld: Crystal Structure of S-Layer Protein Slpa From Lactobacillus Acidophilus, Domain I, Co-Crystallization with HGCL2, Mutation SER146CYS, (Aa 32-198)

The structure of Crystal Structure of S-Layer Protein Slpa From Lactobacillus Acidophilus, Domain I, Co-Crystallization with HGCL2, Mutation SER146CYS, (Aa 32-198), PDB code: 7qld was solved by T.Sagmeister, D.Vejzovic, M.Eder, A.Dordic, T.Pavkov-Keller, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.38 / 2.15
Space group	P 65 2 2
Cell size a, b, c (Å), α, β, γ (°)	85.36, 85.36, 191.965, 90, 90, 120
R / Rfree (%)	21.9 / 26.6

The structure of Crystal Structure of S-Layer Protein Slpa From Lactobacillus Acidophilus, Domain I, Co-Crystallization with HGCL2, Mutation SER146CYS, (Aa 32-198) also contains other interesting chemical elements:

Mercury

(Hg)

2 atoms

The binding sites of Chlorine atom in the Crystal Structure of S-Layer Protein Slpa From Lactobacillus Acidophilus, Domain I, Co-Crystallization with HGCL2, Mutation SER146CYS, (Aa 32-198) (pdb code 7qld). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 4 binding sites of Chlorine where determined in the Crystal Structure of S-Layer Protein Slpa From Lactobacillus Acidophilus, Domain I, Co-Crystallization with HGCL2, Mutation SER146CYS, (Aa 32-198), PDB code: 7qld:
Jump to Chlorine binding site number: 1; 2; 3; 4;

Chlorine binding site 1 out of 4 in the Crystal Structure of S-Layer Protein Slpa From Lactobacillus Acidophilus, Domain I, Co-Crystallization with HGCL2, Mutation SER146CYS, (Aa 32-198)


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 S-Layer Protein Slpa From Lactobacillus Acidophilus, Domain I, Co-Crystallization with HGCL2, Mutation SER146CYS, (Aa 32-198) within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl202 b:64.6 occ:1.00 HG B:HG201 2.5 73.7 0.4 HG21 B:THR55 2.9 47.3 1.0 HA B:THR55 3.0 51.0 1.0 HD2 B:PRO56 3.3 49.1 1.0 HD22 B:ASN148 3.5 68.1 1.0 HB2 B:ASN148 3.5 61.6 1.0 HB B:THR55 3.6 49.1 1.0 CG2 B:THR55 3.8 46.4 1.0 HB3 B:ASN148 3.8 61.6 1.0 CA B:THR55 3.9 52.5 1.0 CB B:THR55 4.0 49.1 1.0 CD B:PRO56 4.1 49.2 1.0 HD3 B:PRO56 4.1 49.1 1.0 CB B:ASN148 4.1 61.0 1.0 O B:HOH344 4.2 54.8 1.0 HG22 B:THR55 4.3 47.2 1.0 O B:PRO56 4.3 54.2 1.0 ND2 B:ASN148 4.3 70.9 1.0 SG B:CYS146 4.4 75.8 1.0 CL B:CL203 4.4 75.1 1.0 HG23 B:THR55 4.4 47.2 1.0 HG22 B:VAL151 4.4 53.8 1.0 N B:PRO56 4.5 48.5 1.0 C B:THR55 4.5 49.3 1.0 HG B:CYS146 4.5 70.8 1.0 O B:VAL54 4.5 48.3 1.0 H B:ASN148 4.6 66.8 1.0 CG B:ASN148 4.8 62.4 1.0

Chlorine binding site 2 out of 4 in the Crystal Structure of S-Layer Protein Slpa From Lactobacillus Acidophilus, Domain I, Co-Crystallization with HGCL2, Mutation SER146CYS, (Aa 32-198)


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 S-Layer Protein Slpa From Lactobacillus Acidophilus, Domain I, Co-Crystallization with HGCL2, Mutation SER146CYS, (Aa 32-198) within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl203 b:75.1 occ:1.00 OD1 B:ASP53 2.3 83.5 1.0 HG B:HG201 2.6 73.7 0.4 H B:ALA147 2.6 67.1 1.0 HG21 B:THR55 3.1 47.3 1.0 CG B:ASP53 3.1 84.7 1.0 OD2 B:ASP53 3.2 97.3 1.0 HA B:CYS146 3.3 65.6 1.0 HB3 B:ALA147 3.4 67.5 1.0 HG23 B:THR55 3.5 47.2 1.0 N B:ALA147 3.5 65.9 1.0 CG2 B:THR55 3.7 46.4 1.0 HB2 B:ALA147 3.8 67.5 1.0 HH B:TYR50 3.9 67.7 0.0 CB B:ALA147 4.0 67.9 1.0 HG22 B:THR55 4.0 47.2 1.0 O B:VAL54 4.1 48.3 1.0 H B:ASN148 4.1 66.8 1.0 CA B:CYS146 4.2 66.0 1.0 C B:CYS146 4.3 70.8 1.0 CA B:ALA147 4.3 66.5 1.0 SG B:CYS146 4.4 75.8 1.0 CL B:CL202 4.4 64.6 1.0 CB B:ASP53 4.6 60.1 1.0 HA B:THR55 4.7 51.0 1.0 OH B:TYR50 4.7 67.5 1.0 C B:VAL54 4.8 50.0 1.0 H B:VAL54 4.8 52.6 1.0 N B:ASN148 4.9 67.6 1.0 HA B:ASP53 4.9 55.7 1.0 HB1 B:ALA147 4.9 67.5 1.0 CB B:CYS146 4.9 62.5 1.0 N B:VAL54 4.9 49.8 1.0 HB2 B:ASP53 5.0 63.7 1.0 HE1 B:TYR50 5.0 68.1 1.0

Chlorine binding site 3 out of 4 in the Crystal Structure of S-Layer Protein Slpa From Lactobacillus Acidophilus, Domain I, Co-Crystallization with HGCL2, Mutation SER146CYS, (Aa 32-198)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Crystal Structure of S-Layer Protein Slpa From Lactobacillus Acidophilus, Domain I, Co-Crystallization with HGCL2, Mutation SER146CYS, (Aa 32-198) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl202 b:103.7 occ:1.00 HA A:SER149 2.6 77.5 1.0 HG A:HG201 2.7 97.2 0.4 HZ1 A:LYS152 2.8 93.6 1.0 HB3 A:SER167 3.0 85.1 1.0 OG A:SER167 3.1 98.2 1.0 HG A:SER167 3.1 101.0 0.0 CB A:SER167 3.4 81.9 1.0 CA A:SER149 3.5 79.9 1.0 HA A:SER167 3.6 75.7 1.0 NZ A:LYS152 3.7 94.7 1.0 HZ2 A:LYS152 3.9 93.7 1.0 O A:VAL151 3.9 68.2 1.0 HB2 A:SER149 4.0 83.1 1.0 CA A:SER167 4.1 80.4 1.0 HB3 A:SER149 4.1 83.1 1.0 O A:SER149 4.1 64.3 1.0 HZ3 A:LYS152 4.1 93.6 1.0 CB A:SER149 4.1 80.8 1.0 O A:ASN148 4.2 90.0 1.0 O A:CYS146 4.2 85.2 1.0 C A:SER149 4.2 62.1 1.0 HD3 A:LYS152 4.2 82.2 1.0 HB2 A:SER167 4.3 85.1 1.0 N A:SER149 4.4 86.7 1.0 O A:SER167 4.6 73.7 1.0 C A:ASN148 4.6 87.1 1.0 HE3 A:LYS152 4.6 90.2 1.0 CE A:LYS152 4.7 91.6 1.0 H A:VAL151 4.7 68.7 1.0 SG A:CYS146 4.8 143.0 1.0 C A:SER167 4.8 69.4 1.0 CL A:CL203 4.9 79.2 0.7 CD A:LYS152 4.9 82.9 1.0

Chlorine binding site 4 out of 4 in the Crystal Structure of S-Layer Protein Slpa From Lactobacillus Acidophilus, Domain I, Co-Crystallization with HGCL2, Mutation SER146CYS, (Aa 32-198)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Crystal Structure of S-Layer Protein Slpa From Lactobacillus Acidophilus, Domain I, Co-Crystallization with HGCL2, Mutation SER146CYS, (Aa 32-198) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl203 b:79.2 occ:0.72 HE2 A:PHE153 2.4 65.1 1.0 CE2 A:PHE153 2.6 68.5 1.0 HG11 A:VAL151 2.6 67.4 1.0 HG A:HG201 2.7 97.2 0.4 O A:SER167 3.0 73.7 1.0 CZ A:PHE153 3.0 60.9 1.0 HB3 A:CYS146 3.0 104.6 1.0 O A:VAL151 3.0 68.2 1.0 HZ A:PHE153 3.1 62.9 1.0 CD2 A:PHE153 3.3 62.9 1.0 HA A:LYS152 3.3 68.5 1.0 HA A:SER167 3.4 75.7 1.0 CG1 A:VAL151 3.5 66.3 1.0 C A:VAL151 3.5 64.0 1.0 HB A:VAL151 3.5 69.7 1.0 HD2 A:PHE153 3.5 65.1 1.0 SG A:CYS146 3.6 143.0 1.0 C A:SER167 3.7 69.4 1.0 CB A:CYS146 3.8 96.7 1.0 HG12 A:VAL151 3.9 67.4 1.0 N A:LYS152 3.9 67.1 1.0 CA A:LYS152 3.9 69.3 1.0 CE1 A:PHE153 3.9 61.7 1.0 HA2 A:GLY145 3.9 73.1 1.0 CB A:VAL151 4.0 69.8 1.0 CA A:SER167 4.1 80.4 1.0 HG13 A:VAL151 4.1 67.4 1.0 CG A:PHE153 4.2 68.1 1.0 N A:CYS146 4.2 73.5 1.0 O A:VAL166 4.2 66.6 1.0 H A:CYS146 4.2 77.2 1.0 C A:GLY145 4.3 72.2 1.0 C A:LYS152 4.3 64.4 1.0 CA A:VAL151 4.3 69.7 1.0 CD1 A:PHE153 4.4 61.5 1.0 HB2 A:CYS146 4.5 104.7 1.0 H A:PHE153 4.5 64.2 1.0 HE1 A:PHE153 4.5 61.7 1.0 H A:LYS152 4.6 66.8 1.0 CA A:CYS146 4.6 91.8 1.0 N A:PHE153 4.6 65.3 1.0 CA A:GLY145 4.6 76.2 1.0 HG A:CYS146 4.6 123.2 1.0 HD3 A:LYS152 4.6 82.2 1.0 HA A:THR168 4.7 67.5 1.0 O A:GLY145 4.7 72.2 1.0 N A:THR168 4.8 66.5 1.0 HB3 A:SER167 4.9 85.1 1.0 CL A:CL202 4.9 103.7 1.0 O A:LYS152 4.9 58.0 1.0 HB A:VAL54 4.9 73.4 1.0 O A:CYS146 5.0 85.2 1.0

T.Sagmeister, M.Eder, C.Grininger, D.Vejzovic, C.Buhlheller, A.Dordic, E.Damisch, C.Millan, A.Medina, I.Uson, M.Baek, R.Read, D.Baker, T.Pavkov-Keller. The Self-Assembly of the S-Layer Protein From Lactobacilli Acidophilus To Be Published.