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Chlorine in PDB 4ilt: Structure of the Dioxygenase Domain of SACTE_2871, A Novel Dioxygenase Carbohydrate-Binding Protein Fusion From the Cellulolytic Bacterium Streptomyces Sp. Sirexaa-E

Protein crystallography data

The structure of Structure of the Dioxygenase Domain of SACTE_2871, A Novel Dioxygenase Carbohydrate-Binding Protein Fusion From the Cellulolytic Bacterium Streptomyces Sp. Sirexaa-E, PDB code: 4ilt was solved by C.M.Bianchetti, T.E.Takasuka, L.F.Bergeman, C.H.Harmann, B.G.Fox, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 42.56 / 2.55
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 49.192, 85.125, 70.264, 90.00, 95.53, 90.00
R / Rfree (%) 20.3 / 26.8

Other elements in 4ilt:

The structure of Structure of the Dioxygenase Domain of SACTE_2871, A Novel Dioxygenase Carbohydrate-Binding Protein Fusion From the Cellulolytic Bacterium Streptomyces Sp. Sirexaa-E also contains other interesting chemical elements:

Iron (Fe) 4 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Structure of the Dioxygenase Domain of SACTE_2871, A Novel Dioxygenase Carbohydrate-Binding Protein Fusion From the Cellulolytic Bacterium Streptomyces Sp. Sirexaa-E (pdb code 4ilt). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Structure of the Dioxygenase Domain of SACTE_2871, A Novel Dioxygenase Carbohydrate-Binding Protein Fusion From the Cellulolytic Bacterium Streptomyces Sp. Sirexaa-E, PDB code: 4ilt:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 4ilt

Go back to Chlorine Binding Sites List in 4ilt
Chlorine binding site 1 out of 2 in the Structure of the Dioxygenase Domain of SACTE_2871, A Novel Dioxygenase Carbohydrate-Binding Protein Fusion From the Cellulolytic Bacterium Streptomyces Sp. Sirexaa-E


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structure of the Dioxygenase Domain of SACTE_2871, A Novel Dioxygenase Carbohydrate-Binding Protein Fusion From the Cellulolytic Bacterium Streptomyces Sp. Sirexaa-E within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl302

b:32.5
occ:1.00
N A:GLY194 3.2 33.0 1.0
ND2 A:ASN198 3.3 35.0 1.0
CA A:GLY194 4.0 29.5 1.0
C A:PRO193 4.1 30.7 1.0
CA A:PRO193 4.2 29.1 1.0
CZ A:PHE204 4.2 29.3 1.0
CG A:ASN198 4.3 29.4 1.0
CB A:ASN198 4.4 28.2 1.0
CD1 A:LEU209 4.4 32.9 1.0
O A:PHE192 4.6 31.5 1.0
CE1 A:PHE204 4.7 34.1 1.0
N A:GLU195 4.8 31.9 1.0
C A:GLY194 4.8 32.4 1.0
CD2 A:LEU209 4.9 29.1 1.0
CE2 A:PHE204 5.0 29.1 1.0

Chlorine binding site 2 out of 2 in 4ilt

Go back to Chlorine Binding Sites List in 4ilt
Chlorine binding site 2 out of 2 in the Structure of the Dioxygenase Domain of SACTE_2871, A Novel Dioxygenase Carbohydrate-Binding Protein Fusion From the Cellulolytic Bacterium Streptomyces Sp. Sirexaa-E


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Structure of the Dioxygenase Domain of SACTE_2871, A Novel Dioxygenase Carbohydrate-Binding Protein Fusion From the Cellulolytic Bacterium Streptomyces Sp. Sirexaa-E within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Cl302

b:31.3
occ:1.00
N D:GLY194 2.9 40.2 1.0
ND2 D:ASN198 3.3 32.1 1.0
CA D:GLY194 3.6 41.5 1.0
C D:PRO193 3.9 39.3 1.0
CA D:PRO193 4.0 38.0 1.0
CZ D:PHE204 4.2 30.7 1.0
CG D:ASN198 4.3 41.8 1.0
CD1 D:LEU209 4.3 33.0 1.0
CB D:ASN198 4.4 43.9 1.0
CE1 D:PHE204 4.5 36.9 1.0
N D:GLU195 4.5 40.7 1.0
C D:GLY194 4.5 42.5 1.0
O D:PHE192 4.5 37.2 1.0
CD2 D:LEU209 4.8 35.8 1.0
CB D:PRO193 5.0 33.7 1.0
O D:GLU195 5.0 46.0 1.0

Reference:

C.M.Bianchetti, C.H.Harmann, T.E.Takasuka, G.L.Hura, K.Dyer, B.G.Fox. Fusion of Dioxygenase and Lignin-Binding Domains in A Novel Secreted Enzyme From Cellulolytic Streptomyces Sp. Sirexaa-E. J.Biol.Chem. V. 288 18574 2013.
ISSN: ISSN 0021-9258
PubMed: 23653358
DOI: 10.1074/JBC.M113.475848
Page generated: Sun Jul 21 16:51:59 2024

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