Zinc 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:

Chlorine

(Cl)

2 atoms

The binding sites of Zinc 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 Zinc atom.
In total 2 binding sites of Zinc where determined in the Clostridium Botulinum Type E Catalytic Domain E212Q Mutant, PDB code: 1t3c:
Jump to Zinc binding site number: 1; 2;

Zinc 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 Zinc with other atoms in the Zn 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:Zn422 b:39.6 occ:1.00 OE2 A:GLU250 2.0 32.1 1.0 NE2 A:HIS215 2.1 31.8 1.0 NE2 A:HIS211 2.2 28.3 1.0 O A:HOH824 2.7 28.2 1.0 CD A:GLU250 2.8 29.9 1.0 OE1 A:GLU250 2.8 34.2 1.0 CD2 A:HIS215 2.9 29.1 1.0 CD2 A:HIS211 3.1 26.2 1.0 CE1 A:HIS215 3.2 27.9 1.0 CE1 A:HIS211 3.3 28.0 1.0 CE1 A:TYR350 3.8 34.0 1.0 OH A:TYR350 3.9 35.2 1.0 CG A:HIS215 4.1 28.1 1.0 CZ A:TYR350 4.2 34.6 1.0 CG A:GLU250 4.2 29.9 1.0 ND1 A:HIS215 4.2 29.9 1.0 CG A:HIS211 4.3 25.6 1.0 ND1 A:HIS211 4.4 29.3 1.0 NE2 A:GLN212 4.4 28.1 1.0 O A:HOH1005 4.7 21.7 1.0 CA A:GLU250 4.7 27.1 1.0 CD1 A:TYR350 4.7 32.2 1.0 CB A:GLU250 4.7 27.6 1.0 OE1 A:GLN212 5.0 26.5 1.0 CG2 A:THR253 5.0 22.9 1.0

Zinc 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 Zinc with other atoms in the Zn binding site number 2 of Clostridium Botulinum Type E Catalytic Domain E212Q Mutant within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn422 b:43.6 occ:1.00 NE2 B:HIS211 1.9 31.4 1.0 OE1 B:GLU250 2.1 41.8 1.0 NE2 B:HIS215 2.1 42.6 1.0 OE2 B:GLU250 2.7 42.5 1.0 CD B:GLU250 2.7 40.8 1.0 O B:HOH602 2.7 62.3 1.0 CE1 B:HIS211 2.8 32.9 1.0 CD2 B:HIS215 3.0 41.5 1.0 CD2 B:HIS211 3.0 30.9 1.0 CE1 B:HIS215 3.2 43.0 1.0 ND1 B:HIS211 4.0 34.2 1.0 CE1 B:TYR350 4.0 48.7 1.0 CG B:HIS211 4.1 31.4 1.0 OH B:TYR350 4.1 48.9 1.0 CG B:HIS215 4.2 39.9 1.0 O B:HOH815 4.2 52.2 1.0 CG B:GLU250 4.2 40.3 1.0 ND1 B:HIS215 4.2 41.9 1.0 NE2 B:GLN212 4.3 35.6 1.0 CZ B:TYR350 4.4 48.2 1.0 O B:HOH759 4.5 49.5 1.0 CA B:GLU250 4.8 37.8 1.0 CB B:GLU250 4.8 39.2 1.0 CG2 B:THR253 4.9 35.0 1.0 CD1 B:TYR350 4.9 49.6 1.0 O B:HOH785 5.0 62.6 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