Chlorine in PDB 8a1k: Crystal Structure of the Transpeptidase LDTMT2 From Mycobacterium Tuberculosis in Complex with Ebsulfur Analogue 15

The structure of Crystal Structure of the Transpeptidase LDTMT2 From Mycobacterium Tuberculosis in Complex with Ebsulfur Analogue 15, PDB code: 8a1k was solved by M.De Munnik, P.A.Lang, J.Brem, C.J.Schofield, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.41 / 1.75
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	60.977, 95.169, 75.624, 90, 92.35, 90
R / Rfree (%)	17.5 / 20.4

The structure of Crystal Structure of the Transpeptidase LDTMT2 From Mycobacterium Tuberculosis in Complex with Ebsulfur Analogue 15 also contains other interesting chemical elements:

Sodium

(Na)

1 atom

The binding sites of Chlorine atom in the Crystal Structure of the Transpeptidase LDTMT2 From Mycobacterium Tuberculosis in Complex with Ebsulfur Analogue 15 (pdb code 8a1k). 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 the Transpeptidase LDTMT2 From Mycobacterium Tuberculosis in Complex with Ebsulfur Analogue 15, PDB code: 8a1k:
Jump to Chlorine binding site number: 1; 2; 3; 4;

Chlorine binding site 1 out of 4 in the Crystal Structure of the Transpeptidase LDTMT2 From Mycobacterium Tuberculosis in Complex with Ebsulfur Analogue 15


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 the Transpeptidase LDTMT2 From Mycobacterium Tuberculosis in Complex with Ebsulfur Analogue 15 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl501 b:29.4 occ:1.00 CL11 A:KT6501 0.0 29.4 1.0 C10 A:KT6501 1.8 23.2 1.0 C09 A:KT6501 2.7 25.4 1.0 C12 A:KT6501 2.7 27.9 1.0 CL13 A:KT6501 3.2 28.0 1.0 CG2 A:THR320 3.2 29.5 0.5 CG1 A:VAL322 3.4 29.5 1.0 O A:HOH975 3.6 19.1 0.5 CH2 A:TRP340 3.7 27.4 1.0 CZ2 A:TRP340 3.7 26.1 1.0 O A:HOH815 3.7 25.6 1.0 O A:HOH1014 3.8 35.9 1.0 CE1 A:HIS336 3.8 24.4 1.0 C08 A:KT6501 4.0 31.4 1.0 C14 A:KT6501 4.0 21.9 1.0 NE2 A:HIS336 4.0 25.1 1.0 CB A:THR320 4.2 34.5 0.5 OG1 A:THR320 4.3 33.0 0.5 C15 A:KT6501 4.5 28.0 1.0 CG A:MET303 4.5 25.3 1.0 ND1 A:HIS336 4.7 23.5 1.0 CB A:MET303 4.7 23.5 1.0 O A:HOH773 4.7 14.3 0.5 CB A:THR320 4.7 38.6 0.5 O A:HOH942 4.8 34.3 1.0 CB A:VAL322 4.8 27.1 1.0 CZ3 A:TRP340 4.8 26.5 1.0 O A:THR320 4.9 26.4 0.5 CG2 A:THR320 4.9 39.8 0.5 CD2 A:HIS336 4.9 23.6 1.0 CE2 A:TRP340 5.0 27.3 1.0

Chlorine binding site 2 out of 4 in the Crystal Structure of the Transpeptidase LDTMT2 From Mycobacterium Tuberculosis in Complex with Ebsulfur Analogue 15


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 the Transpeptidase LDTMT2 From Mycobacterium Tuberculosis in Complex with Ebsulfur Analogue 15 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl501 b:28.0 occ:1.00 CL13 A:KT6501 0.0 28.0 1.0 C12 A:KT6501 1.8 27.9 1.0 C14 A:KT6501 2.7 21.9 1.0 C10 A:KT6501 2.7 23.2 1.0 CL11 A:KT6501 3.2 29.4 1.0 O A:HOH942 3.4 34.3 1.0 O A:HOH773 3.5 14.3 0.5 O A:HOH956 3.5 46.6 1.0 CB A:TYR318 3.5 27.2 1.0 CG A:TYR318 3.6 26.6 1.0 O A:HOH975 3.6 19.1 0.5 O A:HOH1014 3.7 35.9 1.0 ND1 A:HIS352 3.7 27.3 1.0 CD1 A:TYR318 3.8 23.0 1.0 OG1 A:THR320 3.9 33.0 0.5 CG2 A:THR320 3.9 29.5 0.5 C15 A:KT6501 4.0 28.0 1.0 C09 A:KT6501 4.0 25.4 1.0 CE1 A:HIS352 4.1 26.1 1.0 CD2 A:TYR318 4.2 26.8 1.0 C08 A:KT6501 4.5 31.4 1.0 O A:HOH815 4.6 25.6 1.0 CE1 A:TYR318 4.7 23.1 1.0 CG A:HIS352 4.7 28.2 1.0 CB A:THR320 4.8 34.5 0.5 O A:HOH850 4.9 22.8 1.0 O A:HOH852 5.0 30.3 1.0 CE2 A:TYR318 5.0 24.4 1.0 CA A:TYR318 5.0 32.4 1.0

Chlorine binding site 3 out of 4 in the Crystal Structure of the Transpeptidase LDTMT2 From Mycobacterium Tuberculosis in Complex with Ebsulfur Analogue 15


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 the Transpeptidase LDTMT2 From Mycobacterium Tuberculosis in Complex with Ebsulfur Analogue 15 within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl501 b:40.5 occ:1.00 CL11 B:KT6501 0.0 40.5 1.0 C10 B:KT6501 1.8 36.8 1.0 C09 B:KT6501 2.7 40.2 1.0 C12 B:KT6501 2.8 38.1 1.0 CL13 B:KT6501 3.2 42.1 1.0 CG2 B:THR320 3.2 53.9 1.0 O B:HOH875 3.6 39.1 1.0 CZ2 B:TRP340 3.6 43.9 1.0 CH2 B:TRP340 3.7 35.8 1.0 O B:HOH788 3.8 29.5 1.0 CE1 B:HIS336 4.0 32.9 1.0 C08 B:KT6501 4.0 40.2 1.0 C14 B:KT6501 4.0 40.1 1.0 NE2 B:HIS336 4.2 31.2 1.0 C15 B:KT6501 4.6 37.8 1.0 O B:HOH985 4.6 37.8 0.5 CG B:MET303 4.7 44.7 1.0 CB B:VAL322 4.7 44.3 1.0 CB B:THR320 4.7 60.1 1.0 O B:HOH865 4.8 38.2 1.0 ND1 B:HIS336 4.8 33.9 1.0 CE2 B:TRP340 4.8 41.1 1.0 O B:THR320 4.8 43.5 1.0 CB B:MET303 4.9 41.0 1.0 O B:HOH951 4.9 44.9 1.0 CZ3 B:TRP340 5.0 36.7 1.0

Chlorine binding site 4 out of 4 in the Crystal Structure of the Transpeptidase LDTMT2 From Mycobacterium Tuberculosis in Complex with Ebsulfur Analogue 15


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 the Transpeptidase LDTMT2 From Mycobacterium Tuberculosis in Complex with Ebsulfur Analogue 15 within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl501 b:42.1 occ:1.00 CL13 B:KT6501 0.0 42.1 1.0 C12 B:KT6501 1.8 38.1 1.0 C14 B:KT6501 2.7 40.1 1.0 C10 B:KT6501 2.8 36.8 1.0 CL11 B:KT6501 3.2 40.5 1.0 CB B:TYR318 3.4 42.6 1.0 O B:HOH951 3.4 44.9 1.0 CG B:TYR318 3.5 41.4 1.0 O B:HOH865 3.6 38.2 1.0 O B:HOH875 3.7 39.1 1.0 CD1 B:TYR318 3.9 39.4 1.0 ND1 B:HIS352 3.9 37.5 1.0 CG2 B:THR320 4.0 53.9 1.0 C15 B:KT6501 4.0 37.8 1.0 C09 B:KT6501 4.0 40.2 1.0 CD2 B:TYR318 4.1 42.9 1.0 O B:HOH985 4.3 37.8 0.5 CE1 B:HIS352 4.4 43.3 1.0 C08 B:KT6501 4.6 40.2 1.0 O B:HOH788 4.6 29.5 1.0 CE1 B:TYR318 4.8 39.5 1.0 CG B:HIS352 4.8 41.1 1.0 CA B:TYR318 4.8 44.3 1.0 CE2 B:TYR318 4.9 42.4 1.0

M.De Munnik, P.A.Lang, J.Brem, C.J.Schofield. Crystal Structure of the Transpeptidase LDTMT2 From Mycobacterium Tuberculosis in Complex with Ebsulfur Analogue 15 To Be Published.