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

Enzymatic activity of 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;

Protein crystallography data

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

Other elements in 1t3a:

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

Zinc (Zn) 2 atoms

Chlorine Binding Sites:

The binding sites of Chlorine 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 Chlorine atom.
In total only one binding site of Chlorine was determined in the Crystal Structure of Clostridium Botulinum Neurotoxin Type E Catalytic Domain, PDB code: 1t3a:

Chlorine binding site 1 out of 1 in 1t3a

Go back to Chlorine Binding Sites List in 1t3a
Chlorine binding site 1 out of 1 in the Crystal Structure of Clostridium Botulinum Neurotoxin Type E Catalytic Domain


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl 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:Cl501

b:35.7
occ:1.00
 CD A:ARG401 3.6 37.6 1.0
NH1 A:ARG401 3.6 29.4 1.0
O A:HOH554 3.7 22.5 1.0
N A:ILE398 3.8 27.2 1.0
CA A:PRO397 4.0 28.0 1.0
CB A:PRO397 4.4 28.4 1.0
C A:PRO397 4.4 27.4 1.0
CE1 A:PHE357 4.5 25.3 1.0
NE A:ARG401 4.5 38.1 1.0
CB A:ARG401 4.5 35.8 1.0
CZ A:ARG401 4.5 35.7 1.0
CD1 A:PHE357 4.6 24.5 1.0
CG A:ARG401 4.6 38.4 1.0
O A:ILE398 4.7 27.4 1.0
CB A:ILE398 4.7 28.8 1.0
CA A:ILE398 4.8 28.5 1.0
CG1 A:ILE398 5.0 29.6 1.0

Reference:

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
Page generated: Sat Jul 20 02:20:55 2024

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