Atomistry » Chlorine » PDB 6yxi-6zaz » 6za6
Atomistry »
  Chlorine »
    PDB 6yxi-6zaz »
      6za6 »

Chlorine in PDB 6za6: M. Tuberculosis Salicylate Synthase Mbti in Complex with BA2+

Enzymatic activity of M. Tuberculosis Salicylate Synthase Mbti in Complex with BA2+

All present enzymatic activity of M. Tuberculosis Salicylate Synthase Mbti in Complex with BA2+:
4.2.99.21; 5.4.4.2; 5.4.99.5;

Protein crystallography data

The structure of M. Tuberculosis Salicylate Synthase Mbti in Complex with BA2+, PDB code: 6za6 was solved by M.Mori, S.Villa, F.Meneghetti, M.Bellinzoni, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 43.63 / 1.80
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 88.040, 116.900, 94.090, 90.00, 91.60, 90.00
R / Rfree (%) 19.6 / 21.4

Other elements in 6za6:

The structure of M. Tuberculosis Salicylate Synthase Mbti in Complex with BA2+ also contains other interesting chemical elements:

Barium (Ba) 2 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the M. Tuberculosis Salicylate Synthase Mbti in Complex with BA2+ (pdb code 6za6). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 5 binding sites of Chlorine where determined in the M. Tuberculosis Salicylate Synthase Mbti in Complex with BA2+, PDB code: 6za6:
Jump to Chlorine binding site number: 1; 2; 3; 4; 5;

Chlorine binding site 1 out of 5 in 6za6

Go back to Chlorine Binding Sites List in 6za6
Chlorine binding site 1 out of 5 in the M. Tuberculosis Salicylate Synthase Mbti in Complex with BA2+


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of M. Tuberculosis Salicylate Synthase Mbti in Complex with BA2+ within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl503

b:52.0
occ:1.00
 O A:HOH624 2.8 40.2 1.0
NE A:ARG405 3.4 32.3 1.0
O A:HOH755 3.5 47.2 1.0
N A:GLY419 3.5 28.6 1.0
CD A:LYS438 3.6 33.8 1.0
CA A:ALA418 3.7 27.7 1.0
CB A:ALA418 3.9 27.4 1.0
CB A:LEU404 4.0 28.9 1.0
NH2 A:ARG405 4.0 33.9 1.0
OH A:TYR385 4.1 33.7 1.0
C A:ALA418 4.2 28.1 1.0
CZ A:ARG405 4.2 32.8 1.0
CD2 A:LEU404 4.2 31.1 1.0
O A:GLY419 4.2 31.9 1.0
CD A:ARG405 4.3 31.1 1.0
CB A:LYS438 4.3 29.5 1.0
CE1 A:TYR385 4.4 29.5 1.0
CD1 A:LEU404 4.4 30.9 1.0
CG A:LEU404 4.4 30.6 1.0
CG A:LYS438 4.5 31.1 1.0
O A:ARG417 4.5 26.1 1.0
CA A:GLY419 4.5 30.2 1.0
N A:ARG405 4.6 27.6 1.0
CE A:LYS438 4.6 35.3 1.0
NZ A:LYS438 4.7 34.9 1.0
CZ A:TYR385 4.7 31.2 1.0
C A:GLY419 4.8 31.5 1.0
CA A:LEU404 4.8 28.4 1.0
N A:ALA418 4.9 26.6 1.0

Chlorine binding site 2 out of 5 in 6za6

Go back to Chlorine Binding Sites List in 6za6
Chlorine binding site 2 out of 5 in the M. Tuberculosis Salicylate Synthase Mbti in Complex with BA2+


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of M. Tuberculosis Salicylate Synthase Mbti in Complex with BA2+ within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl504

b:37.2
occ:1.00
 O B:HOH660 2.9 43.5 1.0
O B:HOH723 2.9 32.4 1.0
NE B:ARG405 3.4 30.2 1.0
N B:GLY419 3.5 24.3 1.0
O B:HOH694 3.5 37.0 1.0
CD B:LYS438 3.6 23.0 1.0
CA B:ALA418 3.7 23.7 1.0
CB B:ALA418 4.0 23.9 1.0
CB B:LEU404 4.0 24.6 1.0
NH2 B:ARG405 4.0 30.1 1.0
OH B:TYR385 4.1 32.3 1.0
C B:ALA418 4.1 24.0 1.0
O B:GLY419 4.2 23.6 1.0
CZ B:ARG405 4.2 30.0 1.0
CD2 B:LEU404 4.2 27.9 1.0
CD B:ARG405 4.3 28.0 1.0
CD1 B:LEU404 4.4 27.6 1.0
CG B:LEU404 4.4 26.8 1.0
CB B:LYS438 4.4 22.1 1.0
NZ B:LYS438 4.4 25.7 1.0
CE1 B:TYR385 4.4 28.3 1.0
CA B:GLY419 4.5 24.4 1.0
CE B:LYS438 4.5 22.8 1.0
CG B:LYS438 4.5 22.3 1.0
O B:ARG417 4.6 22.8 1.0
N B:ARG405 4.6 23.9 1.0
O B:HOH879 4.6 38.4 1.0
C B:GLY419 4.7 24.1 1.0
CZ B:TYR385 4.8 30.0 1.0
CA B:LEU404 4.8 23.8 1.0
N B:ALA418 4.9 23.4 1.0

Chlorine binding site 3 out of 5 in 6za6

Go back to Chlorine Binding Sites List in 6za6
Chlorine binding site 3 out of 5 in the M. Tuberculosis Salicylate Synthase Mbti in Complex with BA2+


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of M. Tuberculosis Salicylate Synthase Mbti in Complex with BA2+ within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl505

b:32.6
occ:1.00
 NE B:ARG189 3.1 31.6 1.0
NH1 B:ARG189 3.5 30.7 1.0
CZ B:ARG189 3.7 32.4 1.0
CG B:ARG190 4.0 27.1 1.0
CG2 B:VAL193 4.1 30.2 1.0
CD B:ARG189 4.1 31.2 1.0
CG B:ARG189 4.5 30.4 1.0
CA B:ARG190 4.7 26.1 1.0
CD B:ARG190 4.9 28.4 1.0
N B:ARG190 4.9 26.3 1.0
CB B:ARG190 4.9 25.8 1.0

Chlorine binding site 4 out of 5 in 6za6

Go back to Chlorine Binding Sites List in 6za6
Chlorine binding site 4 out of 5 in the M. Tuberculosis Salicylate Synthase Mbti in Complex with BA2+


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of M. Tuberculosis Salicylate Synthase Mbti in Complex with BA2+ within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cl503

b:48.4
occ:1.00
 O C:HOH750 2.8 37.1 1.0
N C:GLY419 3.3 32.9 1.0
O C:HOH723 3.3 41.1 1.0
OH C:TYR385 3.6 33.5 1.0
CA C:ALA418 3.7 31.2 1.0
NE C:ARG405 3.8 35.7 1.0
CD C:LYS438 3.9 31.3 1.0
C C:ALA418 4.0 31.7 1.0
CD2 C:LEU404 4.0 29.7 1.0
CB C:LEU404 4.0 27.3 1.0
CB C:ALA418 4.1 31.4 1.0
CE1 C:TYR385 4.1 32.1 1.0
O C:GLY419 4.1 34.4 1.0
CA C:GLY419 4.2 34.4 1.0
CZ C:TYR385 4.3 33.0 1.0
NH2 C:ARG405 4.3 36.4 1.0
CG C:LEU404 4.3 29.0 1.0
CD1 C:LEU404 4.4 29.8 1.0
CZ C:ARG405 4.5 36.6 1.0
O C:ARG417 4.5 29.2 1.0
C C:GLY419 4.6 34.9 1.0
CB C:LYS438 4.7 28.4 1.0
CD C:ARG405 4.7 35.7 1.0
NZ C:LYS438 4.7 34.4 1.0
N C:ARG405 4.7 28.3 1.0
CE C:LYS438 4.8 33.8 1.0
CG C:LYS438 4.8 29.7 1.0
CA C:LEU404 4.8 26.9 1.0
N C:ALA418 4.9 30.0 1.0

Chlorine binding site 5 out of 5 in 6za6

Go back to Chlorine Binding Sites List in 6za6
Chlorine binding site 5 out of 5 in the M. Tuberculosis Salicylate Synthase Mbti in Complex with BA2+


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 5 of M. Tuberculosis Salicylate Synthase Mbti in Complex with BA2+ within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Cl504

b:39.5
occ:1.00
 O D:HOH678 2.9 39.1 1.0
NE D:ARG405 3.3 36.9 1.0
N D:GLY419 3.5 32.3 1.0
CD D:LYS438 3.5 37.7 1.0
O D:HOH690 3.6 40.3 1.0
CA D:ALA418 3.8 32.8 1.0
NH2 D:ARG405 3.9 38.1 1.0
CB D:ALA418 3.9 33.4 1.0
CB D:LEU404 4.0 30.7 1.0
CZ D:ARG405 4.0 37.6 1.0
C D:ALA418 4.2 32.6 1.0
CD2 D:LEU404 4.2 32.4 1.0
CD D:ARG405 4.2 36.5 1.0
O D:GLY419 4.2 35.0 1.0
CB D:LYS438 4.3 33.4 1.0
CD1 D:LEU404 4.3 33.4 1.0
CG D:LEU404 4.4 32.1 1.0
NZ D:LYS438 4.4 38.3 1.0
CG D:LYS438 4.5 35.1 1.0
CE D:LYS438 4.5 38.4 1.0
CA D:GLY419 4.5 33.5 1.0
N D:ARG405 4.5 30.0 1.0
OH D:TYR385 4.6 35.0 1.0
O D:ARG417 4.6 31.5 1.0
CE1 D:TYR385 4.6 31.6 1.0
C D:GLY419 4.8 34.6 1.0
O D:HOH808 4.8 35.7 1.0
CA D:LEU404 4.8 30.1 1.0

Reference:

M.Mori, G.Stelitano, A.Gelain, E.Pini, L.R.Chiarelli, J.C.Sammartino, G.Poli, T.Tuccinardi, G.Beretta, A.Porta, M.Bellinzoni, S.Villa, F.Meneghetti. Shedding X-Ray Light on the Role of Magnesium in the Activity Ofmycobacterium Tuberculosissalicylate Synthase (Mbti) For Drug Design. J.Med.Chem. V. 63 7066 2020.
ISSN: ISSN 0022-2623
PubMed: 32530281
DOI: 10.1021/ACS.JMEDCHEM.0C00373
Page generated: Mon Jul 29 18:00:51 2024

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy