Chlorine in PDB 1t3c: Clostridium Botulinum Type E Catalytic Domain E212Q Mutant

All present enzymatic activity of Clostridium Botulinum Type E Catalytic Domain E212Q Mutant:
3.4.24.69;

The structure of Clostridium Botulinum Type E Catalytic Domain E212Q Mutant, PDB code: 1t3c was solved by R.Agarwal, S.Eswaramoorthy, D.Kumaran, T.Binz, S.Swaminathan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.26 / 1.90
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	88.208, 144.297, 82.589, 90.00, 90.00, 90.00
R / Rfree (%)	24.5 / 29.5

The structure of Clostridium Botulinum Type E Catalytic Domain E212Q Mutant also contains other interesting chemical elements:

Zinc

(Zn)

2 atoms

The binding sites of Chlorine atom in the Clostridium Botulinum Type E Catalytic Domain E212Q Mutant (pdb code 1t3c). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Clostridium Botulinum Type E Catalytic Domain E212Q Mutant, PDB code: 1t3c:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Clostridium Botulinum Type E Catalytic Domain E212Q Mutant


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Clostridium Botulinum Type E Catalytic Domain E212Q Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl623 b:13.8 occ:1.00 NH1 A:ARG401 3.5 41.8 1.0 CD A:ARG401 3.5 39.0 1.0 O A:HOH892 3.5 22.0 1.0 N A:ILE398 3.7 26.0 1.0 CA A:PRO397 4.1 28.2 1.0 CD1 A:PHE357 4.3 21.7 1.0 CE1 A:PHE357 4.3 23.9 1.0 CZ A:ARG401 4.4 39.2 1.0 NE A:ARG401 4.4 39.7 1.0 CB A:ARG401 4.4 34.9 1.0 C A:PRO397 4.4 27.6 1.0 CB A:ILE398 4.5 28.1 1.0 CG A:ARG401 4.5 38.5 1.0 CG1 A:ILE398 4.7 26.9 1.0 CB A:PRO397 4.7 29.5 1.0 CA A:ILE398 4.7 28.5 1.0 O A:ILE398 4.7 30.5 1.0

Chlorine binding site 2 out of 2 in the Clostridium Botulinum Type E Catalytic Domain E212Q Mutant


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Clostridium Botulinum Type E Catalytic Domain E212Q Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl823 b:11.7 occ:1.00 NZ A:LYS61 2.7 50.4 1.0 CE A:LYS61 3.5 48.1 1.0 O A:HOH1068 3.7 41.0 1.0 CD A:LYS61 3.9 46.0 1.0 CG A:LYS61 4.6 41.7 1.0

R.Agarwal, S.Eswaramoorthy, D.Kumaran, T.Binz, S.Swaminathan. Structural Analysis of Botulinum Neurotoxin Type E Catalytic Domain and Its Mutant GLU212-->Gln Reveals the Pivotal Role of the GLU212 Carboxylate in the Catalytic Pathway Biochemistry V. 43 6637 2004.
ISSN: ISSN 0006-2960
PubMed: 15157097
DOI: 10.1021/BI036278W