Bromine in PDB 2vps: Structure of the Bifunctional Leishmania Major Trypanothione Synthetase-Amidase

All present enzymatic activity of Structure of the Bifunctional Leishmania Major Trypanothione Synthetase-Amidase:
6.3.1.9;

The structure of Structure of the Bifunctional Leishmania Major Trypanothione Synthetase-Amidase, PDB code: 2vps was solved by P.K.Fyfe, S.L.Oza, A.H.Fairlamb, W.N.Hunter, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	28.33 / 2.75
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	71.050, 85.600, 168.340, 90.00, 90.00, 90.00
R / Rfree (%)	20.4 / 25

The structure of Structure of the Bifunctional Leishmania Major Trypanothione Synthetase-Amidase also contains other interesting chemical elements:

Chlorine

(Cl)

5 atoms

The binding sites of Bromine atom in the Structure of the Bifunctional Leishmania Major Trypanothione Synthetase-Amidase (pdb code 2vps). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total 2 binding sites of Bromine where determined in the Structure of the Bifunctional Leishmania Major Trypanothione Synthetase-Amidase, PDB code: 2vps:
Jump to Bromine binding site number: 1; 2;

Bromine binding site 1 out of 2 in the Structure of the Bifunctional Leishmania Major Trypanothione Synthetase-Amidase


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of Structure of the Bifunctional Leishmania Major Trypanothione Synthetase-Amidase within 5.0Å range: probe atom residue distance (Å) B Occ A:Br1657 b:71.1 occ:1.00 CG A:ARG6 3.6 46.9 1.0 NH2 A:ARG452 3.8 53.7 1.0 NE A:ARG6 3.9 48.4 1.0 CB A:ARG6 3.9 46.7 1.0 CA A:ARG6 4.2 47.1 1.0 CD A:ARG6 4.3 47.6 1.0 NH1 A:ARG452 4.4 54.5 1.0 N A:ALA7 4.5 47.4 1.0 CZ A:ARG452 4.6 54.1 1.0 OG1 A:THR395 4.8 55.5 1.0 C A:ARG6 4.9 46.9 1.0 CZ A:ARG6 4.9 48.3 1.0 NH2 A:ARG6 5.0 49.5 1.0

Bromine binding site 2 out of 2 in the Structure of the Bifunctional Leishmania Major Trypanothione Synthetase-Amidase


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 2 of Structure of the Bifunctional Leishmania Major Trypanothione Synthetase-Amidase within 5.0Å range: probe atom residue distance (Å) B Occ A:Br1658 b:0.4 occ:1.00 NH1 A:ARG328 3.6 62.5 1.0 NH2 A:ARG328 4.0 61.5 1.0 OG A:SER351 4.1 67.5 1.0 N A:SER351 4.2 68.3 1.0 CZ A:ARG328 4.3 61.3 1.0 CB A:SER351 4.4 67.6 1.0 CA A:SER351 4.9 67.6 1.0

P.K.Fyfe, S.L.Oza, A.H.Fairlamb, W.N.Hunter. Leishmania Trypanothione Synthetase-Amidase Structure Reveals A Basis For Regulation of Conflicting Synthetic and Hydrolytic Activities. J.Biol.Chem. V. 283 17672 2008.
ISSN: ISSN 0021-9258
PubMed: 18420578
DOI: 10.1074/JBC.M801850200