Zinc in PDB 1t3a: Crystal Structure of Clostridium Botulinum Neurotoxin Type E Catalytic Domain

All present enzymatic activity of Crystal Structure of Clostridium Botulinum Neurotoxin Type E Catalytic Domain:
3.4.24.69;

The structure of Crystal Structure of Clostridium Botulinum Neurotoxin Type E Catalytic Domain, PDB code: 1t3a 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)	41.69 / 2.16
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	88.330, 144.456, 83.271, 90.00, 90.00, 90.00
R / Rfree (%)	22.5 / 25.8

The structure of Crystal Structure of Clostridium Botulinum Neurotoxin Type E Catalytic Domain also contains other interesting chemical elements:

Chlorine

(Cl)

1 atom

The binding sites of Zinc atom in the Crystal Structure of Clostridium Botulinum Neurotoxin Type E Catalytic Domain (pdb code 1t3a). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of Clostridium Botulinum Neurotoxin Type E Catalytic Domain, PDB code: 1t3a:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of Clostridium Botulinum Neurotoxin Type E Catalytic Domain


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Clostridium Botulinum Neurotoxin Type E Catalytic Domain within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn422 b:31.9 occ:1.00 NE2 A:HIS215 2.0 25.1 1.0 O A:HOH502 2.1 30.8 1.0 NE2 A:HIS211 2.1 28.3 1.0 OE2 A:GLU250 2.1 29.3 1.0 CD A:GLU250 2.8 27.8 1.0 OE1 A:GLU250 2.9 30.9 1.0 CD2 A:HIS215 2.9 22.6 1.0 CD2 A:HIS211 2.9 23.7 1.0 CE1 A:HIS215 3.2 22.6 1.0 CE1 A:HIS211 3.2 26.2 1.0 OH A:TYR350 3.9 38.9 1.0 OE2 A:GLU212 3.9 28.0 1.0 CE1 A:TYR350 3.9 36.0 1.0 CG A:HIS215 4.1 24.5 1.0 CG A:HIS211 4.2 24.1 1.0 CZ A:TYR350 4.2 36.8 1.0 ND1 A:HIS215 4.2 27.6 1.0 ND1 A:HIS211 4.3 27.8 1.0 CG A:GLU250 4.3 28.3 1.0 O A:HOH533 4.7 18.0 1.0 CD A:GLU212 4.7 24.0 1.0 CA A:GLU250 4.7 26.6 1.0 OE1 A:GLU212 4.8 28.2 1.0 CB A:GLU250 4.8 26.0 1.0 CD1 A:TYR350 4.8 35.3 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of Clostridium Botulinum Neurotoxin Type E Catalytic Domain


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of Clostridium Botulinum Neurotoxin Type E Catalytic Domain within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn422 b:45.9 occ:1.00 NE2 B:HIS211 2.0 30.9 1.0 NE2 B:HIS215 2.1 42.0 1.0 OE1 B:GLU250 2.1 36.5 1.0 O B:HOH451 2.2 47.3 1.0 OE2 B:GLU250 2.7 36.1 1.0 CD B:GLU250 2.7 38.3 1.0 CD2 B:HIS215 2.9 39.6 1.0 CD2 B:HIS211 2.9 30.5 1.0 CE1 B:HIS211 3.1 33.1 1.0 CE1 B:HIS215 3.2 40.6 1.0 CG B:HIS215 4.1 39.1 1.0 CG B:HIS211 4.1 31.8 1.0 OE2 B:GLU212 4.2 41.5 1.0 ND1 B:HIS211 4.2 33.1 1.0 CG B:GLU250 4.2 38.9 1.0 O B:HOH526 4.2 55.4 1.0 ND1 B:HIS215 4.2 40.2 1.0 CE1 B:TYR350 4.3 53.3 1.0 OH B:TYR350 4.4 53.7 1.0 O B:HOH517 4.6 37.7 1.0 CZ B:TYR350 4.6 52.9 1.0 CA B:GLU250 4.7 39.1 1.0 CB B:GLU250 4.8 39.8 1.0 CG2 B:THR253 4.8 36.1 1.0 CD B:GLU212 4.9 39.7 1.0 OE1 B:GLU212 5.0 39.5 1.0 CB B:THR253 5.0 38.8 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