Chlorine in PDB 3u9f: Structure of Cati in Complex with Chloramphenicol

All present enzymatic activity of Structure of Cati in Complex with Chloramphenicol:
2.3.1.28;

The structure of Structure of Cati in Complex with Chloramphenicol, PDB code: 3u9f was solved by T.Biswas, S.Garneau-Tsodikova, O.V.Tsodikov, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	35.00 / 2.90
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	107.336, 114.429, 114.374, 119.97, 97.83, 98.64
R / Rfree (%)	23.6 / 30.9

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 20; Page 3, Binding sites: 21 - 30; Page 4, Binding sites: 31 - 36;

Binding sites:

The binding sites of Chlorine atom in the Structure of Cati in Complex with Chloramphenicol (pdb code 3u9f). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 36 binding sites of Chlorine where determined in the Structure of Cati in Complex with Chloramphenicol, PDB code: 3u9f:
Jump to Chlorine binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Chlorine binding site 1 out of 36 in the Structure of Cati in Complex with Chloramphenicol


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structure of Cati in Complex with Chloramphenicol within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl221 b:71.5 occ:1.00 CL1 A:CLM221 0.0 71.5 1.0 C1 A:CLM221 1.8 71.6 1.0 C2 A:CLM221 2.7 70.1 1.0 N2 A:CLM221 2.9 68.4 1.0 CL2 A:CLM221 3.0 74.5 1.0 OG A:SER104 3.3 59.7 1.0 CD2 A:PHE144 3.6 52.2 1.0 O2 A:CLM221 3.8 70.5 1.0 CG2 A:THR93 4.0 55.4 1.0 CB A:SER104 4.1 60.3 1.0 C11 A:CLM221 4.2 67.4 1.0 CB A:PHE144 4.2 51.1 1.0 C3 A:CLM221 4.3 67.7 1.0 CG A:PHE144 4.3 51.5 1.0 O5 A:CLM221 4.4 66.6 1.0 CE2 A:PHE144 4.4 53.1 1.0 SG A:CYS91 4.4 56.4 1.0 O A:CYS91 4.5 55.0 1.0 C5 A:CLM221 4.7 66.9 1.0 C6 A:CLM221 4.8 67.2 1.0 O A:VAL145 4.8 51.6 1.0 C10 A:CLM221 4.9 68.0 1.0

Chlorine binding site 2 out of 36 in the Structure of Cati in Complex with Chloramphenicol


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Structure of Cati in Complex with Chloramphenicol within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl221 b:74.5 occ:1.00 CL2 A:CLM221 0.0 74.5 1.0 C1 A:CLM221 1.8 71.6 1.0 C2 A:CLM221 2.7 70.1 1.0 O2 A:CLM221 2.9 70.5 1.0 CL1 A:CLM221 3.0 71.5 1.0 OH A:TYR133 3.2 60.0 1.0 CZ A:PHE134 3.4 61.5 1.0 OG A:SER104 3.6 59.7 1.0 N2 A:CLM221 3.9 68.4 1.0 CZ A:TYR133 4.0 62.2 1.0 CE1 A:PHE134 4.2 61.8 1.0 CE2 A:PHE134 4.2 62.3 1.0 CB A:SER104 4.2 60.3 1.0 CE2 A:PHE144 4.2 53.1 1.0 CD2 A:PHE144 4.3 52.2 1.0 CE2 A:TYR133 4.4 62.3 1.0 C11 A:CLM221 4.6 67.4 1.0 C10 A:CLM221 4.7 68.0 1.0 CE1 A:TYR133 4.8 63.4 1.0

Chlorine binding site 3 out of 36 in the Structure of Cati in Complex with Chloramphenicol


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Structure of Cati in Complex with Chloramphenicol within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl221 b:58.9 occ:1.00 CL1 B:CLM221 0.0 58.9 1.0 C1 B:CLM221 1.8 59.2 1.0 C2 B:CLM221 2.7 57.8 1.0 N2 B:CLM221 2.9 56.1 1.0 CL2 B:CLM221 2.9 62.8 1.0 OG B:SER104 3.1 57.2 1.0 CG2 B:THR93 3.6 55.5 1.0 CD2 B:PHE144 3.7 53.4 1.0 O2 B:CLM221 3.8 58.1 1.0 CB B:SER104 4.0 57.7 1.0 O5 B:CLM221 4.3 52.9 1.0 C3 B:CLM221 4.3 54.6 1.0 C11 B:CLM221 4.3 53.2 1.0 CE2 B:PHE144 4.3 54.4 1.0 O B:VAL145 4.5 52.7 1.0 CG B:PHE144 4.6 52.6 1.0 SG B:CYS91 4.6 57.0 1.0 CB B:PHE144 4.7 52.0 1.0 O B:CYS91 4.7 54.8 1.0 C5 B:CLM221 4.7 53.5 1.0 C6 B:CLM221 4.8 53.6 1.0

Chlorine binding site 4 out of 36 in the Structure of Cati in Complex with Chloramphenicol


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Structure of Cati in Complex with Chloramphenicol within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl221 b:62.8 occ:1.00 CL2 B:CLM221 0.0 62.8 1.0 C1 B:CLM221 1.8 59.2 1.0 C2 B:CLM221 2.7 57.8 1.0 O2 B:CLM221 2.8 58.1 1.0 CL1 B:CLM221 2.9 58.9 1.0 OH B:TYR133 3.2 55.9 1.0 CZ B:PHE134 3.3 56.5 1.0 OG B:SER104 3.7 57.2 1.0 CE2 B:PHE134 3.9 57.5 1.0 N2 B:CLM221 3.9 56.1 1.0 CZ B:TYR133 4.0 57.3 1.0 CE2 B:PHE144 4.0 54.4 1.0 CB B:SER104 4.2 57.7 1.0 CD2 B:PHE144 4.3 53.4 1.0 CE2 B:TYR133 4.3 57.5 1.0 CE1 B:PHE134 4.4 57.0 1.0 C11 B:CLM221 4.7 53.2 1.0 C10 B:CLM221 4.8 53.5 1.0 CE1 B:TYR133 4.9 58.5 1.0 CZ B:PHE144 5.0 54.4 1.0

Chlorine binding site 5 out of 36 in the Structure of Cati in Complex with Chloramphenicol


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 5 of Structure of Cati in Complex with Chloramphenicol within 5.0Å range: probe atom residue distance (Å) B Occ C:Cl221 b:71.0 occ:1.00 CL1 C:CLM221 0.0 71.0 1.0 C1 C:CLM221 1.8 70.5 1.0 C2 C:CLM221 2.7 69.1 1.0 N2 C:CLM221 2.7 66.8 1.0 CL2 C:CLM221 3.0 73.1 1.0 OG C:SER104 3.0 51.8 1.0 CG2 C:THR93 3.5 51.9 1.0 O2 C:CLM221 3.9 69.6 1.0 CD2 C:PHE144 3.9 55.3 1.0 CB C:SER104 4.0 52.4 1.0 O5 C:CLM221 4.0 63.2 1.0 C3 C:CLM221 4.1 65.0 1.0 C11 C:CLM221 4.3 62.2 1.0 SG C:CYS91 4.5 51.8 1.0 C5 C:CLM221 4.5 63.5 1.0 O C:CYS91 4.6 50.1 1.0 CE2 C:PHE144 4.6 56.0 1.0 C6 C:CLM221 4.7 63.0 1.0 O C:VAL145 4.7 53.8 1.0 CE2 C:PHE102 4.7 52.6 1.0 CG C:PHE144 4.7 54.6 1.0 CB C:PHE144 4.7 53.9 1.0 C4 C:CLM221 4.8 64.8 1.0 CB C:THR93 5.0 52.8 1.0

Chlorine binding site 6 out of 36 in the Structure of Cati in Complex with Chloramphenicol


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 6 of Structure of Cati in Complex with Chloramphenicol within 5.0Å range: probe atom residue distance (Å) B Occ C:Cl221 b:73.1 occ:1.00 CL2 C:CLM221 0.0 73.1 1.0 C1 C:CLM221 1.8 70.5 1.0 C2 C:CLM221 2.7 69.1 1.0 CL1 C:CLM221 3.0 71.0 1.0 O2 C:CLM221 3.0 69.6 1.0 OH C:TYR133 3.4 59.2 1.0 CZ C:PHE134 3.5 56.4 1.0 N2 C:CLM221 3.8 66.8 1.0 CE2 C:PHE144 4.1 56.0 1.0 OG C:SER104 4.2 51.8 1.0 CZ C:TYR133 4.2 59.4 1.0 CD2 C:PHE144 4.3 55.3 1.0 CE2 C:PHE134 4.3 57.1 1.0 CE1 C:PHE134 4.4 56.0 1.0 C11 C:CLM221 4.5 62.2 1.0 C10 C:CLM221 4.5 62.9 1.0 CB C:SER104 4.6 52.4 1.0 CE2 C:TYR133 4.7 58.9 1.0 C6 C:CLM221 4.8 63.0 1.0 C9 C:CLM221 4.8 63.7 1.0 C3 C:CLM221 4.9 65.0 1.0 CZ C:PHE144 5.0 55.8 1.0

Chlorine binding site 7 out of 36 in the Structure of Cati in Complex with Chloramphenicol


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 7 of Structure of Cati in Complex with Chloramphenicol within 5.0Å range: probe atom residue distance (Å) B Occ D:Cl221 b:64.3 occ:1.00 CL1 D:CLM221 0.0 64.3 1.0 C1 D:CLM221 1.8 63.5 1.0 C2 D:CLM221 2.7 61.7 1.0 N2 D:CLM221 2.7 59.5 1.0 CL2 D:CLM221 3.0 65.8 1.0 OG D:SER104 3.6 65.1 1.0 CD2 D:PHE144 3.6 63.2 1.0 CG2 D:THR93 3.7 60.4 1.0 O2 D:CLM221 3.8 62.3 1.0 C3 D:CLM221 4.1 57.7 1.0 CB D:SER104 4.2 66.1 1.0 CE2 D:PHE144 4.4 63.9 1.0 CG D:PHE144 4.4 62.2 1.0 CB D:PHE144 4.4 61.6 1.0 C11 D:CLM221 4.5 53.6 1.0 O5 D:CLM221 4.5 56.3 1.0 C6 D:CLM221 4.6 54.5 1.0 C5 D:CLM221 4.6 55.6 1.0 C4 D:CLM221 4.7 58.2 1.0 SG D:CYS91 4.9 62.1 1.0 O D:CYS91 4.9 60.4 1.0 O D:VAL145 5.0 63.4 1.0

Chlorine binding site 8 out of 36 in the Structure of Cati in Complex with Chloramphenicol


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 8 of Structure of Cati in Complex with Chloramphenicol within 5.0Å range: probe atom residue distance (Å) B Occ D:Cl221 b:65.8 occ:1.00 CL2 D:CLM221 0.0 65.8 1.0 C1 D:CLM221 1.8 63.5 1.0 C2 D:CLM221 2.7 61.7 1.0 CL1 D:CLM221 3.0 64.3 1.0 OH D:TYR133 3.0 65.8 1.0 O2 D:CLM221 3.1 62.3 1.0 N2 D:CLM221 3.6 59.5 1.0 CE2 D:PHE144 3.8 63.9 1.0 CD2 D:PHE144 3.9 63.2 1.0 C9 D:CLM221 4.0 54.3 1.0 CZ D:TYR133 4.1 67.5 1.0 C10 D:CLM221 4.1 53.7 1.0 C8 D:CLM221 4.1 54.3 1.0 CZ D:PHE134 4.1 68.5 1.0 C7 D:CLM221 4.2 54.4 1.0 C11 D:CLM221 4.2 53.6 1.0 C6 D:CLM221 4.3 54.5 1.0 CE2 D:PHE134 4.4 69.4 1.0 OG D:SER104 4.4 65.1 1.0 N9 D:CLM221 4.6 55.2 1.0 CZ D:PHE144 4.6 63.4 1.0 CE1 D:TYR133 4.7 68.4 1.0 O9A D:CLM221 4.7 56.0 1.0 C3 D:CLM221 4.7 57.7 1.0 CG D:PHE144 4.8 62.2 1.0 CE2 D:TYR133 5.0 68.8 1.0

Chlorine binding site 9 out of 36 in the Structure of Cati in Complex with Chloramphenicol


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 9 of Structure of Cati in Complex with Chloramphenicol within 5.0Å range: probe atom residue distance (Å) B Occ E:Cl221 b:65.8 occ:1.00 CL1 E:CLM221 0.0 65.8 1.0 C1 E:CLM221 1.8 65.6 1.0 C2 E:CLM221 2.7 64.0 1.0 N2 E:CLM221 2.8 61.1 1.0 CL2 E:CLM221 3.0 67.9 1.0 OG E:SER104 3.3 60.9 1.0 CB E:SER104 3.7 60.7 1.0 CG2 E:THR93 3.8 57.4 1.0 O2 E:CLM221 3.9 65.7 1.0 CD2 E:PHE144 4.0 52.2 1.0 C3 E:CLM221 4.3 59.0 1.0 SG E:CYS91 4.5 55.1 1.0 O E:CYS91 4.7 53.6 1.0 CB E:PHE144 4.7 51.4 1.0 CE2 E:PHE144 4.7 53.1 1.0 CG E:PHE144 4.7 51.2 1.0 CA E:SER104 4.8 62.3 1.0 C11 E:CLM221 4.9 54.7 1.0 CE2 E:PHE102 4.9 60.0 1.0 C4 E:CLM221 4.9 59.4 1.0 C6 E:CLM221 4.9 55.5 1.0 O5 E:CLM221 5.0 56.4 1.0 C5 E:CLM221 5.0 56.8 1.0

Chlorine binding site 10 out of 36 in the Structure of Cati in Complex with Chloramphenicol


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 10 of Structure of Cati in Complex with Chloramphenicol within 5.0Å range: probe atom residue distance (Å) B Occ E:Cl221 b:67.9 occ:1.00 CL2 E:CLM221 0.0 67.9 1.0 C1 E:CLM221 1.8 65.6 1.0 C2 E:CLM221 2.7 64.0 1.0 CL1 E:CLM221 3.0 65.8 1.0 O2 E:CLM221 3.2 65.7 1.0 OH E:TYR133 3.4 61.4 1.0 N2 E:CLM221 3.6 61.1 1.0 CZ E:PHE134 4.0 61.2 1.0 C9 E:CLM221 4.1 55.0 1.0 C8 E:CLM221 4.1 55.2 1.0 O9A E:CLM221 4.2 56.6 1.0 C10 E:CLM221 4.2 54.4 1.0 CD2 E:PHE144 4.3 52.2 1.0 CE2 E:PHE144 4.3 53.1 1.0 C7 E:CLM221 4.3 55.3 1.0 C11 E:CLM221 4.4 54.7 1.0 C6 E:CLM221 4.4 55.5 1.0 CZ E:TYR133 4.4 63.3 1.0 OG E:SER104 4.4 60.9 1.0 CE2 E:PHE134 4.5 62.0 1.0 N9 E:CLM221 4.6 55.6 1.0 C3 E:CLM221 4.7 59.0 1.0 CB E:SER104 4.9 60.7 1.0 CE1 E:PHE134 5.0 61.7 1.0

T.Biswas, J.L.Houghton, S.Garneau-Tsodikova, O.V.Tsodikov. The Structural Basis For Substrate Versatility of Chloramphenicol Acetyltransferase Cat(I). Protein Sci. V. 21 520 2012.
ISSN: ISSN 0961-8368
PubMed: 22294317
DOI: 10.1002/PRO.2036