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

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: 4ilv 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)	32.81 / 2.06
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	62.463, 62.463, 195.997, 90.00, 90.00, 90.00
R / Rfree (%)	18.3 / 23.7

The binding sites of Iron 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 4ilv). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron 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: 4ilv:
Jump to Iron binding site number: 1; 2;

Iron 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 Iron with other atoms in the Fe 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:Fe301 b:29.8 occ:1.00 OH A:TYR138 2.0 23.1 1.0 OH A:TYR167 2.1 33.7 1.0 NE2 A:HIS173 2.2 29.9 1.0 NE2 A:HIS175 2.3 25.4 1.0 O2 A:EDO302 2.4 33.1 1.0 O1 A:EDO302 2.4 32.2 1.0 CZ A:TYR138 3.0 22.8 1.0 CE1 A:HIS173 3.0 30.5 1.0 C2 A:EDO302 3.1 32.9 1.0 CD2 A:HIS175 3.2 22.8 1.0 CZ A:TYR167 3.2 30.5 1.0 CD2 A:HIS173 3.2 27.6 1.0 CE1 A:HIS175 3.2 26.8 1.0 C1 A:EDO302 3.3 37.7 1.0 CE2 A:TYR138 3.6 24.7 1.0 CE2 A:TYR167 3.7 29.4 1.0 CE1 A:TYR138 4.0 22.5 1.0 O A:HOH410 4.1 20.6 1.0 NH1 A:ARG170 4.2 33.5 1.0 ND1 A:HIS173 4.2 27.9 1.0 CG A:HIS173 4.3 24.8 1.0 ND1 A:HIS175 4.4 27.7 1.0 CE1 A:TYR167 4.4 30.1 1.0 CG A:HIS175 4.4 29.0 1.0 O A:HOH444 4.5 34.6 1.0 CD2 A:TYR87 4.8 56.4 1.0 CD2 A:TYR138 4.8 24.9 1.0 CD A:ARG170 5.0 34.5 1.0

Iron 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 Iron with other atoms in the Fe 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 B:Fe301 b:28.4 occ:1.00 OH B:TYR138 1.9 27.9 1.0 OH B:TYR167 2.1 32.0 1.0 NE2 B:HIS173 2.2 26.4 1.0 NE2 B:HIS175 2.2 28.0 1.0 O2 B:EDO302 2.3 27.6 1.0 O1 B:EDO302 2.5 33.6 1.0 CZ B:TYR138 2.9 34.4 1.0 CE1 B:HIS173 3.1 18.8 1.0 CE1 B:HIS175 3.2 35.1 1.0 C2 B:EDO302 3.2 34.7 1.0 CD2 B:HIS173 3.2 26.2 1.0 CD2 B:HIS175 3.2 25.7 1.0 CZ B:TYR167 3.3 32.1 1.0 C1 B:EDO302 3.3 39.0 1.0 CE2 B:TYR138 3.6 28.8 1.0 CE2 B:TYR167 3.8 27.5 1.0 CE1 B:TYR138 3.9 34.2 1.0 NH1 B:ARG170 4.2 32.4 1.0 O B:HOH402 4.2 21.3 1.0 ND1 B:HIS173 4.2 24.6 1.0 ND1 B:HIS175 4.3 31.3 1.0 CG B:HIS173 4.3 24.9 1.0 CG B:HIS175 4.4 30.8 1.0 CE1 B:TYR167 4.4 31.7 1.0 CD2 B:TYR87 4.6 34.0 1.0 O B:HOH405 4.8 32.5 1.0 CD2 B:TYR138 4.9 30.1 1.0

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