Platinum in PDB 7kem: Crystallographic Structure of L,D-Transpeptidase 2 From Mycobacterium Tuberculosis

The structure of Crystallographic Structure of L,D-Transpeptidase 2 From Mycobacterium Tuberculosis, PDB code: 7kem was solved by G.A.Libreros, M.V.B.Dias, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	49.66 / 1.77
Space group	I 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	117.528, 121.051, 122.699, 90.00, 90.00, 90.00
R / Rfree (%)	26.1 / 27.5

The structure of Crystallographic Structure of L,D-Transpeptidase 2 From Mycobacterium Tuberculosis also contains other interesting chemical elements:

Iodine

(I)

11 atoms

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 12;

Binding sites:

The binding sites of Platinum atom in the Crystallographic Structure of L,D-Transpeptidase 2 From Mycobacterium Tuberculosis (pdb code 7kem). This binding sites where shown within 5.0 Angstroms radius around Platinum atom.
In total 12 binding sites of Platinum where determined in the Crystallographic Structure of L,D-Transpeptidase 2 From Mycobacterium Tuberculosis, PDB code: 7kem:
Jump to Platinum binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Platinum binding site 1 out of 12 in the Crystallographic Structure of L,D-Transpeptidase 2 From Mycobacterium Tuberculosis


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Stereo pair view

A full contact list of Platinum with other atoms in the Pt binding site number 1 of Crystallographic Structure of L,D-Transpeptidase 2 From Mycobacterium Tuberculosis within 5.0Å range: probe atom residue distance (Å) B Occ A:Pt501 b:41.1 occ:0.00 PT1 A:0JC501 0.0 41.1 0.0 N2 A:0JC501 2.0 43.7 0.0 N1 A:0JC501 2.0 46.9 0.0 I1 A:0JC501 2.4 50.5 0.0 ND1 A:HIS347 2.6 32.6 1.0 C2 A:0JC501 2.7 44.0 0.0 C1 A:0JC501 2.9 47.3 0.0 CB A:HIS347 3.2 22.5 1.0 CG A:HIS347 3.3 27.2 1.0 CA A:HIS347 3.3 23.0 1.0 CE1 A:HIS347 3.7 32.1 1.0 O A:HIS347 3.8 23.7 1.0 C A:HIS347 4.0 22.4 1.0 O A:GLY346 4.1 24.8 1.0 N A:HIS347 4.5 20.9 1.0 CD2 A:HIS347 4.6 31.2 1.0 C A:GLY346 4.8 23.4 1.0 NE2 A:HIS347 4.8 35.2 1.0

Platinum binding site 2 out of 12 in the Crystallographic Structure of L,D-Transpeptidase 2 From Mycobacterium Tuberculosis


Mono view


Stereo pair view

A full contact list of Platinum with other atoms in the Pt binding site number 2 of Crystallographic Structure of L,D-Transpeptidase 2 From Mycobacterium Tuberculosis within 5.0Å range: probe atom residue distance (Å) B Occ A:Pt502 b:0.9 occ:0.00 PT1 A:0JC502 0.0 0.9 0.0 SD A:MET157 0.4 35.6 0.5 CE A:MET157 1.7 35.3 0.5 CG A:MET157 1.9 29.1 0.5 N1 A:0JC502 2.0 96.2 0.0 N2 A:0JC502 2.1 94.0 0.0 CG A:MET157 2.1 30.1 0.5 PT1 A:0JC502 2.3 45.8 0.0 I1 A:0JC502 2.7 0.3 0.0 CB A:MET157 2.7 27.2 0.5 CB A:MET157 2.7 27.8 0.5 C1 A:0JC502 2.7 93.9 0.0 C2 A:0JC502 2.9 93.1 0.0 N2 A:0JC502 3.2 52.6 0.0 SD A:MET157 3.4 36.8 0.5 I1 A:0JC502 3.5 79.7 0.0 CA A:MET157 4.2 24.9 0.5 CA A:MET157 4.2 25.1 0.5 N1 A:0JC502 4.3 51.1 0.0 CD A:ARG173 4.4 55.9 1.0 C2 A:0JC502 4.4 48.8 0.0 NH2 A:ARG371 4.5 43.8 1.0 N A:MET157 4.6 23.6 0.5 N A:MET157 4.6 23.4 0.5 CE A:MET157 4.7 34.0 0.5 CB A:ALA171 4.9 23.0 1.0

Platinum binding site 3 out of 12 in the Crystallographic Structure of L,D-Transpeptidase 2 From Mycobacterium Tuberculosis


Mono view


Stereo pair view

A full contact list of Platinum with other atoms in the Pt binding site number 3 of Crystallographic Structure of L,D-Transpeptidase 2 From Mycobacterium Tuberculosis within 5.0Å range: probe atom residue distance (Å) B Occ A:Pt502 b:45.8 occ:0.00 PT1 A:0JC502 0.0 45.8 0.0 I1 A:0JC502 1.8 0.3 0.0 N2 A:0JC502 2.1 52.6 0.0 N1 A:0JC502 2.1 51.1 0.0 PT1 A:0JC502 2.3 0.9 0.0 I1 A:0JC502 2.7 79.7 0.0 SD A:MET157 2.7 35.6 0.5 C2 A:0JC502 2.9 48.8 0.0 C1 A:0JC502 3.0 48.9 0.0 CE A:MET157 3.0 35.3 0.5 NH2 A:ARG371 3.2 43.8 1.0 CB A:MET157 3.5 27.2 0.5 CB A:MET157 3.5 27.8 0.5 CG A:MET157 3.5 29.1 0.5 CG A:MET157 3.6 30.1 0.5 N1 A:0JC502 3.8 96.2 0.0 N2 A:0JC502 4.1 94.0 0.0 CZ A:ARG371 4.2 52.1 1.0 SD A:MET157 4.2 36.8 0.5 NE A:ARG371 4.7 48.7 1.0 OH A:TYR330 4.8 41.2 1.0 C1 A:0JC502 4.9 93.9 0.0 CA A:MET157 5.0 24.9 0.5 CA A:MET157 5.0 25.1 0.5 OE2 A:GLU168 5.0 28.6 1.0

Platinum binding site 4 out of 12 in the Crystallographic Structure of L,D-Transpeptidase 2 From Mycobacterium Tuberculosis


Mono view


Stereo pair view

A full contact list of Platinum with other atoms in the Pt binding site number 4 of Crystallographic Structure of L,D-Transpeptidase 2 From Mycobacterium Tuberculosis within 5.0Å range: probe atom residue distance (Å) B Occ A:Pt503 b:60.6 occ:0.00 PT1 A:0JC503 0.0 60.6 0.0 N1 A:0JC503 2.0 63.1 0.0 N2 A:0JC503 2.1 63.6 0.0 CE A:MET237 2.2 71.0 1.0 I1 A:0JC503 2.5 70.0 0.0 C1 A:0JC503 2.8 62.1 0.0 C2 A:0JC503 2.9 61.7 0.0 SD A:MET237 3.7 84.0 1.0 CG A:MET237 3.7 62.1 1.0 CA A:HIS150 4.4 40.5 1.0 CB A:HIS150 5.0 42.9 1.0 N A:HIS150 5.0 41.1 1.0

Platinum binding site 5 out of 12 in the Crystallographic Structure of L,D-Transpeptidase 2 From Mycobacterium Tuberculosis


Mono view


Stereo pair view

A full contact list of Platinum with other atoms in the Pt binding site number 5 of Crystallographic Structure of L,D-Transpeptidase 2 From Mycobacterium Tuberculosis within 5.0Å range: probe atom residue distance (Å) B Occ A:Pt504 b:0.6 occ:0.00 PT1 A:0JC504 0.0 0.6 0.0 PT1 A:0JC504 0.6 0.2 0.0 N2 A:0JC504 1.9 94.8 0.0 N1 A:0JC504 2.0 95.9 0.0 N1 A:0JC504 2.1 90.2 0.0 N2 A:0JC504 2.1 88.8 0.0 I1 A:0JC504 2.7 0.5 0.0 C2 A:0JC504 2.7 92.7 0.0 C1 A:0JC504 2.9 92.2 0.0 C2 A:0JC504 3.0 87.4 0.0 C1 A:0JC504 3.1 87.0 0.0 I1 A:0JC504 3.1 1.0 0.0 CA A:HIS214 3.5 26.1 1.0 ND1 A:HIS214 3.5 39.3 1.0 CB A:HIS214 3.8 29.0 1.0 N A:PHE215 3.8 22.8 1.0 CG A:HIS214 4.0 38.8 1.0 O A:GLU213 4.1 27.9 1.0 C A:HIS214 4.2 23.8 1.0 CE1 A:HIS214 4.5 43.5 1.0 N A:HIS214 4.6 25.5 1.0 CG A:PHE215 4.7 21.9 1.0 C A:GLU213 4.8 28.6 1.0 CD1 A:PHE215 4.9 21.3 1.0 CD2 A:PHE215 4.9 22.4 1.0

Platinum binding site 6 out of 12 in the Crystallographic Structure of L,D-Transpeptidase 2 From Mycobacterium Tuberculosis


Mono view


Stereo pair view

A full contact list of Platinum with other atoms in the Pt binding site number 6 of Crystallographic Structure of L,D-Transpeptidase 2 From Mycobacterium Tuberculosis within 5.0Å range: probe atom residue distance (Å) B Occ A:Pt504 b:0.2 occ:0.00 PT1 A:0JC504 0.0 0.2 0.0 PT1 A:0JC504 0.6 0.6 0.0 N2 A:0JC504 1.8 88.8 0.0 N1 A:0JC504 2.1 95.9 0.0 N2 A:0JC504 2.1 94.8 0.0 N1 A:0JC504 2.1 90.2 0.0 C2 A:0JC504 2.6 87.4 0.0 I1 A:0JC504 2.7 1.0 0.0 C1 A:0JC504 2.9 87.0 0.0 C2 A:0JC504 3.0 92.7 0.0 C1 A:0JC504 3.1 92.2 0.0 I1 A:0JC504 3.1 0.5 0.0 ND1 A:HIS214 3.6 39.3 1.0 CA A:HIS214 4.0 26.1 1.0 CB A:HIS214 4.2 29.0 1.0 CG A:HIS214 4.3 38.8 1.0 O A:GLU213 4.3 27.9 1.0 N A:PHE215 4.5 22.8 1.0 CE1 A:HIS214 4.5 43.5 1.0 C A:HIS214 4.7 23.8 1.0 N A:HIS214 4.9 25.5 1.0

Platinum binding site 7 out of 12 in the Crystallographic Structure of L,D-Transpeptidase 2 From Mycobacterium Tuberculosis


Mono view


Stereo pair view

A full contact list of Platinum with other atoms in the Pt binding site number 7 of Crystallographic Structure of L,D-Transpeptidase 2 From Mycobacterium Tuberculosis within 5.0Å range: probe atom residue distance (Å) B Occ B:Pt502 b:73.6 occ:0.00 CE B:MET237 2.0 58.0 1.0 N B:HIS150 3.4 60.9 1.0 SD B:MET237 3.6 65.5 0.8 CG B:MET237 3.9 56.9 1.0 CA B:HIS150 4.8 56.9 1.0

Platinum binding site 8 out of 12 in the Crystallographic Structure of L,D-Transpeptidase 2 From Mycobacterium Tuberculosis


Mono view


Stereo pair view

A full contact list of Platinum with other atoms in the Pt binding site number 8 of Crystallographic Structure of L,D-Transpeptidase 2 From Mycobacterium Tuberculosis within 5.0Å range: probe atom residue distance (Å) B Occ B:Pt503 b:53.1 occ:0.00 PT1 B:0JC503 0.0 53.1 0.0 N2 B:0JC503 2.1 57.7 0.0 N1 B:0JC503 2.1 59.4 0.0 ND1 B:HIS347 2.1 33.2 1.0 I1 B:0JC503 2.6 76.3 0.0 C2 B:0JC503 2.8 57.1 0.0 C1 B:0JC503 2.9 57.5 0.0 CE1 B:HIS347 3.1 33.9 1.0 CG B:HIS347 3.2 27.5 1.0 CB B:HIS347 3.5 24.1 1.0 CA B:HIS347 3.7 22.9 1.0 O B:GLY346 3.9 22.6 1.0 NE2 B:HIS347 4.2 29.4 1.0 CD2 B:HIS347 4.3 28.7 1.0 O B:HIS347 4.6 20.2 1.0 C B:HIS347 4.7 21.9 1.0 N B:HIS347 4.7 20.1 1.0 C B:GLY346 4.7 22.1 1.0

Platinum binding site 9 out of 12 in the Crystallographic Structure of L,D-Transpeptidase 2 From Mycobacterium Tuberculosis


Mono view


Stereo pair view

A full contact list of Platinum with other atoms in the Pt binding site number 9 of Crystallographic Structure of L,D-Transpeptidase 2 From Mycobacterium Tuberculosis within 5.0Å range: probe atom residue distance (Å) B Occ B:Pt504 b:0.8 occ:0.00 PT1 B:0JC504 0.0 0.8 0.0 N2 B:0JC504 2.0 0.6 0.0 N1 B:0JC504 2.0 0.5 0.0 I1 B:0JC504 2.6 0.7 0.0 C2 B:0JC504 2.8 0.2 0.0 C1 B:0JC504 2.8 0.3 0.0 O B:GLU213 3.7 31.0 1.0 ND1 B:HIS214 3.8 40.2 1.0 CA B:HIS214 3.8 29.4 1.0 CB B:HIS214 4.4 33.1 1.0 CG B:HIS214 4.4 42.4 1.0 N B:PHE215 4.4 25.6 1.0 C B:GLU213 4.6 29.1 1.0 C B:HIS214 4.6 27.9 1.0 CE1 B:HIS214 4.6 46.8 1.0 N B:HIS214 4.7 27.1 1.0 CE3 B:TRP394 4.7 24.2 1.0 CZ3 B:TRP394 4.8 24.9 1.0

Platinum binding site 10 out of 12 in the Crystallographic Structure of L,D-Transpeptidase 2 From Mycobacterium Tuberculosis


Mono view


Stereo pair view

A full contact list of Platinum with other atoms in the Pt binding site number 10 of Crystallographic Structure of L,D-Transpeptidase 2 From Mycobacterium Tuberculosis within 5.0Å range: probe atom residue distance (Å) B Occ B:Pt505 b:5.1 occ:0.00 PT1 B:0JC505 0.0 5.1 0.0 N2 B:0JC505 0.7 5.7 0.0 PT1 B:0JC505 1.3 54.2 0.0 N1 B:0JC505 2.0 33.1 0.0 N2 B:0JC505 2.0 25.5 0.0 C2 B:0JC505 2.1 36.2 0.0 I1 B:0JC505 2.6 19.7 0.0 N1 B:0JC505 2.7 59.0 0.0 C1 B:0JC505 2.8 31.3 0.0 C1 B:0JC505 2.9 26.7 0.0 C2 B:0JC505 2.9 36.2 0.0 SD B:MET157 3.4 63.6 1.0 I1 B:0JC505 3.9 75.0 0.0 CB B:MET157 4.0 28.1 1.0 CG B:MET157 4.1 42.6 1.0 CE B:MET157 4.1 54.2 1.0 NH2 B:ARG371 4.5 71.6 1.0 OE2 B:GLU168 4.7 26.7 1.0 CD B:ARG371 4.8 51.7 1.0 CZ B:ARG371 4.8 67.3 1.0 NE B:ARG371 4.9 57.7 1.0

G.A.Libreros, M.V.B.Dias. Crystallographic Structure of L,D-Transpeptidase 2 From Mycobacterium Tuberculosis. To Be Published.