Iron in PDB 5jso: Structures of Dddq From Ruegeria Lac. Reveal Key Residues For Metal Binding and Catalysis - Tris Bound

All present enzymatic activity of Structures of Dddq From Ruegeria Lac. Reveal Key Residues For Metal Binding and Catalysis - Tris Bound:
4.4.1.3;

The structure of Structures of Dddq From Ruegeria Lac. Reveal Key Residues For Metal Binding and Catalysis - Tris Bound, PDB code: 5jso was solved by A.E.Brummett, M.Dey, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.82 / 2.00
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	46.870, 87.761, 48.900, 90.00, 93.37, 90.00
R / Rfree (%)	18.5 / 23.6

The structure of Structures of Dddq From Ruegeria Lac. Reveal Key Residues For Metal Binding and Catalysis - Tris Bound also contains other interesting chemical elements:

Chlorine

(Cl)

5 atoms

The binding sites of Iron atom in the Structures of Dddq From Ruegeria Lac. Reveal Key Residues For Metal Binding and Catalysis - Tris Bound (pdb code 5jso). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Structures of Dddq From Ruegeria Lac. Reveal Key Residues For Metal Binding and Catalysis - Tris Bound, PDB code: 5jso:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Structures of Dddq From Ruegeria Lac. Reveal Key Residues For Metal Binding and Catalysis - Tris Bound


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structures of Dddq From Ruegeria Lac. Reveal Key Residues For Metal Binding and Catalysis - Tris Bound within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe301 b:13.8 occ:1.00 NE2 A:HIS125 2.1 14.0 1.0 OE1 A:GLU129 2.2 12.6 1.0 NE2 A:HIS163 2.2 17.8 1.0 OE2 A:GLU129 2.3 13.9 1.0 O1 A:TRS302 2.4 27.1 1.0 CD A:GLU129 2.6 15.1 1.0 C1 A:TRS302 2.7 24.5 1.0 CE1 A:HIS125 3.0 21.3 1.0 OH A:TYR131 3.1 17.5 0.3 CD2 A:HIS125 3.1 15.8 1.0 CE1 A:HIS163 3.1 14.7 1.0 CD2 A:HIS163 3.2 14.2 1.0 NE2 A:HIS123 3.8 18.0 1.0 CZ A:TYR131 3.9 15.8 0.3 CD2 A:HIS123 3.9 19.3 1.0 CG A:GLU129 4.1 11.8 1.0 ND1 A:HIS125 4.1 14.9 1.0 CE2 A:TYR131 4.2 12.9 0.3 CG A:HIS125 4.2 13.4 1.0 ND1 A:HIS163 4.2 20.1 1.0 CE1 A:TYR131 4.2 16.4 0.7 C A:TRS302 4.2 19.7 1.0 CG A:HIS163 4.3 15.6 1.0 ND1 A:HIS157 4.5 14.8 1.0 CB A:GLU129 4.6 11.5 1.0 NE1 A:TRP178 4.6 13.3 1.0 OH A:TYR131 4.8 13.1 0.7 C3 A:TRS302 4.9 21.4 1.0 CE1 A:TYR131 4.9 13.5 0.3 N A:TRS302 4.9 35.4 1.0

Iron binding site 2 out of 2 in the Structures of Dddq From Ruegeria Lac. Reveal Key Residues For Metal Binding and Catalysis - Tris Bound


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Structures of Dddq From Ruegeria Lac. Reveal Key Residues For Metal Binding and Catalysis - Tris Bound within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe301 b:14.4 occ:1.00 NE2 B:HIS125 2.1 13.3 1.0 OE1 B:GLU129 2.2 18.8 1.0 OE2 B:GLU129 2.2 15.6 1.0 O1 B:TRS302 2.3 27.6 1.0 NE2 B:HIS163 2.3 17.1 1.0 CD B:GLU129 2.5 17.1 1.0 C1 B:TRS302 2.7 29.2 1.0 CD2 B:HIS125 3.0 18.7 1.0 OH B:TYR131 3.1 18.6 0.3 CE1 B:HIS125 3.1 19.1 1.0 CE1 B:HIS163 3.2 17.3 1.0 CD2 B:HIS163 3.3 16.5 1.0 NE2 B:HIS123 3.7 20.2 1.0 CZ B:TYR131 3.9 16.4 0.3 CD2 B:HIS123 3.9 19.9 1.0 CG B:GLU129 4.0 15.2 1.0 CE2 B:TYR131 4.1 14.6 0.3 ND1 B:HIS125 4.2 17.9 1.0 CG B:HIS125 4.2 16.1 1.0 CE1 B:TYR131 4.2 16.1 0.7 C B:TRS302 4.2 19.0 1.0 ND1 B:HIS163 4.3 17.9 1.0 CG B:HIS163 4.4 19.9 1.0 NE1 B:TRP178 4.5 16.6 1.0 ND1 B:HIS157 4.5 17.7 1.0 CB B:GLU129 4.6 12.2 1.0 OH B:TYR131 4.7 13.5 0.7 N B:TRS302 4.8 38.8 1.0 CE1 B:TYR131 4.9 14.9 0.3 CZ B:TYR131 4.9 14.3 0.7 CE1 B:HIS123 4.9 19.6 1.0 C3 B:TRS302 5.0 21.4 1.0

A.E.Brummett, M.Dey. New Mechanistic Insight From Substrate- and Product-Bound Structures of the Metal-Dependent Dimethylsulfoniopropionate Lyase Dddq. Biochemistry V. 55 6162 2016.
ISSN: ISSN 1520-4995
PubMed: 27755868
DOI: 10.1021/ACS.BIOCHEM.6B00585