Chlorine in PDB 2fs7: Crystal Structure of Apo-Cellular Retinoic Acid Binding Protein Type II at 1.55 Angstroms Resolution

The structure of Crystal Structure of Apo-Cellular Retinoic Acid Binding Protein Type II at 1.55 Angstroms Resolution, PDB code: 2fs7 was solved by S.Vaezeslami, J.H.Geiger, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 1.55
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	34.475, 37.220, 57.597, 73.09, 75.74, 87.22
R / Rfree (%)	14.4 / 20.1

The binding sites of Chlorine atom in the Crystal Structure of Apo-Cellular Retinoic Acid Binding Protein Type II at 1.55 Angstroms Resolution (pdb code 2fs7). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 5 binding sites of Chlorine where determined in the Crystal Structure of Apo-Cellular Retinoic Acid Binding Protein Type II at 1.55 Angstroms Resolution, PDB code: 2fs7:
Jump to Chlorine binding site number: 1; 2; 3; 4; 5;

Chlorine binding site 1 out of 5 in the Crystal Structure of Apo-Cellular Retinoic Acid Binding Protein Type II at 1.55 Angstroms 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 Apo-Cellular Retinoic Acid Binding Protein Type II at 1.55 Angstroms Resolution within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl501 b:30.5 occ:1.00 OH A:TYR134 2.8 19.9 1.0 O A:HOH763 3.3 46.4 1.0 NH2 A:ARG132 3.5 20.7 1.0 O A:HOH661 3.5 29.7 0.0 CG2 A:THR54 3.6 19.2 1.0 CG A:PRO39 3.8 20.6 1.0 CZ A:TYR134 3.8 17.0 1.0 CB A:PRO39 3.8 19.5 1.0 NE A:ARG132 3.9 18.1 1.0 CE2 A:TYR134 3.9 16.2 1.0 CG2 A:VAL41 4.1 18.8 1.0 CZ A:ARG132 4.2 19.4 1.0 CB A:THR54 4.9 18.1 1.0 OG1 A:THR54 5.0 21.1 1.0

Chlorine binding site 2 out of 5 in the Crystal Structure of Apo-Cellular Retinoic Acid Binding Protein Type II at 1.55 Angstroms 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 Apo-Cellular Retinoic Acid Binding Protein Type II at 1.55 Angstroms Resolution within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl504 b:21.7 occ:1.00 O A:HOH630 3.0 23.9 1.0 OG A:SER12 3.0 16.6 1.0 O A:HOH636 3.3 34.7 0.5 N A:PHE15 3.4 14.8 1.0 N A:ASN14 3.5 15.5 1.0 O A:SER12 3.5 16.7 1.0 C A:SER12 3.6 14.6 1.0 CB A:PHE15 3.6 16.2 1.0 N A:GLU13 3.7 14.4 1.0 C A:GLU13 3.7 14.0 1.0 CB A:SER12 3.7 16.3 1.0 CA A:GLU13 3.8 15.6 1.0 O A:HOH636 3.9 17.3 0.5 CA A:PHE15 4.1 14.8 1.0 CA A:SER12 4.3 14.7 1.0 C A:ASN14 4.4 15.7 1.0 CA A:ASN14 4.4 14.7 1.0 O A:GLU13 4.4 14.6 1.0 O A:HOH645 4.6 24.2 1.0 N A:GLU16 4.7 15.4 1.0 CG A:PHE15 4.9 16.1 1.0 C A:PHE15 4.9 15.4 1.0

Chlorine binding site 3 out of 5 in the Crystal Structure of Apo-Cellular Retinoic Acid Binding Protein Type II at 1.55 Angstroms Resolution


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 Apo-Cellular Retinoic Acid Binding Protein Type II at 1.55 Angstroms Resolution within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl502 b:26.9 occ:0.50 CL B:CL502 0.0 26.9 0.5 CL B:CL502 1.5 29.3 0.5 O B:HOH618 2.7 23.8 1.0 NH2 B:ARG111 3.0 21.3 1.0 O B:HOH730 3.1 44.5 1.0 NE B:ARG111 3.2 18.5 1.0 CZ B:ARG111 3.5 21.0 1.0 CG2 B:VAL41 3.6 21.5 1.0 CD2 B:LEU121 3.8 17.9 1.0 CB B:LEU121 4.0 16.3 1.0 CG1 B:VAL41 4.0 21.0 1.0 CE1 B:TYR134 4.1 18.4 1.0 CD1 B:LEU121 4.2 18.1 1.0 CG B:LEU121 4.2 16.8 1.0 CB B:VAL41 4.4 22.0 1.0 CD B:ARG111 4.5 18.1 1.0 CZ B:TYR134 4.5 19.1 1.0 OH B:TYR134 4.6 23.4 1.0 CD1 B:TYR134 4.8 17.5 1.0 CD2 B:LEU119 4.8 18.9 1.0 NH1 B:ARG111 4.9 20.1 1.0 OG1 B:THR54 4.9 25.6 1.0 CG B:ARG111 4.9 15.5 1.0

Chlorine binding site 4 out of 5 in the Crystal Structure of Apo-Cellular Retinoic Acid Binding Protein Type II at 1.55 Angstroms Resolution


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 Apo-Cellular Retinoic Acid Binding Protein Type II at 1.55 Angstroms Resolution within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl502 b:29.3 occ:0.50 CL B:CL502 0.0 29.3 0.5 CL B:CL502 1.5 26.9 0.5 NE B:ARG111 2.7 18.5 1.0 CD B:ARG111 3.5 18.1 1.0 CD2 B:LEU119 3.5 18.9 1.0 NH2 B:ARG111 3.5 21.3 1.0 CZ B:ARG111 3.6 21.0 1.0 CG B:ARG111 3.9 15.5 1.0 CB B:LEU121 3.9 16.3 1.0 CG B:LEU119 4.1 19.7 1.0 CG1 B:VAL41 4.1 21.0 1.0 O B:HOH618 4.1 23.8 1.0 CD1 B:LEU121 4.3 18.1 1.0 CG2 B:VAL41 4.4 21.5 1.0 CD1 B:LEU119 4.4 20.9 1.0 CE1 B:TYR134 4.4 18.4 1.0 CG B:LEU121 4.5 16.8 1.0 O B:HOH730 4.6 44.5 1.0 CD2 B:LEU121 4.6 17.9 1.0 CD1 B:TYR134 4.6 17.5 1.0 CB B:VAL41 4.7 22.0 1.0 CA B:LEU121 4.8 16.4 1.0 NH1 B:ARG111 4.8 20.1 1.0 CD1 B:ILE43 4.9 19.5 1.0 N B:LEU121 5.0 16.0 1.0

Chlorine binding site 5 out of 5 in the Crystal Structure of Apo-Cellular Retinoic Acid Binding Protein Type II at 1.55 Angstroms Resolution


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 5 of Crystal Structure of Apo-Cellular Retinoic Acid Binding Protein Type II at 1.55 Angstroms Resolution within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl503 b:25.1 occ:1.00 OG B:SER12 2.9 25.1 1.0 NE B:ARG132 3.1 21.0 1.0 N B:LYS38 3.2 24.2 1.0 O B:HOH710 3.3 51.8 1.0 NH2 B:ARG132 3.5 20.7 1.0 CZ B:ARG132 3.7 20.5 1.0 CB B:PHE15 3.7 17.0 1.0 CB B:SER12 3.8 20.6 1.0 CG B:PHE15 3.8 17.0 1.0 CA B:SER37 3.9 22.8 1.0 CB B:SER37 3.9 23.3 1.0 CA B:LYS38 4.0 25.2 1.0 C B:SER37 4.1 23.9 1.0 CD B:ARG132 4.1 18.9 1.0 CG B:LYS38 4.1 30.7 1.0 CD2 B:PHE15 4.1 18.8 1.0 CD1 B:PHE15 4.3 17.1 1.0 CG B:ARG132 4.3 17.5 1.0 O B:HOH606 4.3 19.4 1.0 CB B:LYS38 4.7 26.9 1.0 CE2 B:PHE15 4.8 19.8 1.0 CD B:PRO39 4.8 24.0 1.0 CE1 B:PHE15 4.9 19.2 1.0 CD1 B:ILE9 5.0 22.7 1.0

S.Vaezeslami, E.Mathes, C.Vasileiou, B.Borhan, J.H.Geiger. The Structure of Apo-Wild-Type Cellular Retinoic Acid Binding Protein II at 1.4 A and Its Relationship to Ligand Binding and Nuclear Translocation. J.Mol.Biol. V. 363 687 2006.
ISSN: ISSN 0022-2836
PubMed: 16979656
DOI: 10.1016/J.JMB.2006.08.059