Iron in PDB 3t67: Axial Ligand Swapping in Double Mutant Maintains Intradiol-Cleavage Chemistry in Protocatechuate 3,4-Dioxygenase

All present enzymatic activity of Axial Ligand Swapping in Double Mutant Maintains Intradiol-Cleavage Chemistry in Protocatechuate 3,4-Dioxygenase:
1.13.11.3;

The structure of Axial Ligand Swapping in Double Mutant Maintains Intradiol-Cleavage Chemistry in Protocatechuate 3,4-Dioxygenase, PDB code: 3t67 was solved by V.M.Purpero, J.D.Lipscomb, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.68 / 1.67
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	128.009, 140.782, 168.189, 90.00, 90.00, 90.00
R / Rfree (%)	16.5 / 18.9

The binding sites of Iron atom in the Axial Ligand Swapping in Double Mutant Maintains Intradiol-Cleavage Chemistry in Protocatechuate 3,4-Dioxygenase (pdb code 3t67). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 3 binding sites of Iron where determined in the Axial Ligand Swapping in Double Mutant Maintains Intradiol-Cleavage Chemistry in Protocatechuate 3,4-Dioxygenase, PDB code: 3t67:
Jump to Iron binding site number: 1; 2; 3;

Iron binding site 1 out of 3 in the Axial Ligand Swapping in Double Mutant Maintains Intradiol-Cleavage Chemistry in Protocatechuate 3,4-Dioxygenase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Axial Ligand Swapping in Double Mutant Maintains Intradiol-Cleavage Chemistry in Protocatechuate 3,4-Dioxygenase within 5.0Å range: probe atom residue distance (Å) B Occ M:Fe600 b:18.0 occ:0.70 OH M:TYR408 1.9 21.1 1.0 NE2 M:HIS460 2.1 15.9 1.0 O4 M:CAQ1 2.1 24.6 1.0 OH M:TYR447 2.2 19.0 0.5 NE2 M:HIS462 2.2 15.3 1.0 O3 M:CAQ1 2.5 30.3 1.0 C4 M:CAQ1 2.9 28.2 1.0 CE1 M:HIS460 2.9 16.5 1.0 CZ M:TYR408 3.0 17.7 1.0 CE1 M:HIS462 3.1 15.8 1.0 C3 M:CAQ1 3.1 28.1 1.0 CD2 M:HIS460 3.2 15.8 1.0 CD2 M:HIS462 3.2 16.0 1.0 CZ M:TYR447 3.4 17.6 0.5 CE2 M:TYR408 3.7 17.7 1.0 CE2 M:TYR447 3.8 18.0 0.5 CE1 M:TYR408 3.9 18.0 1.0 O M:HOH794 4.1 18.2 1.0 ND1 M:HIS460 4.1 15.1 1.0 O M:HOH233 4.1 16.4 1.0 NH1 M:ARG457 4.2 16.0 1.0 C5 M:CAQ1 4.2 29.0 1.0 ND1 M:HIS462 4.2 14.5 1.0 CG M:HIS460 4.3 14.8 1.0 O A:HOH238 4.3 18.6 1.0 CG M:HIS462 4.3 14.8 1.0 C2 M:CAQ1 4.4 29.1 1.0 CE1 M:TYR447 4.5 18.7 0.5 OE1 M:GLN477 4.8 17.0 1.0

Iron binding site 2 out of 3 in the Axial Ligand Swapping in Double Mutant Maintains Intradiol-Cleavage Chemistry in Protocatechuate 3,4-Dioxygenase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Axial Ligand Swapping in Double Mutant Maintains Intradiol-Cleavage Chemistry in Protocatechuate 3,4-Dioxygenase within 5.0Å range: probe atom residue distance (Å) B Occ N:Fe600 b:17.2 occ:0.70 OH N:TYR408 1.9 20.8 1.0 O4 N:CAQ1 2.1 23.7 1.0 NE2 N:HIS462 2.1 16.3 1.0 NE2 N:HIS460 2.1 15.7 1.0 OH N:TYR447 2.2 19.4 0.5 O3 N:CAQ1 2.3 30.6 1.0 C4 N:CAQ1 2.8 28.0 1.0 CE1 N:HIS460 3.0 17.3 1.0 C3 N:CAQ1 3.0 28.5 1.0 CZ N:TYR408 3.0 18.8 1.0 CE1 N:HIS462 3.0 15.9 1.0 CD2 N:HIS462 3.2 15.3 1.0 CD2 N:HIS460 3.3 16.8 1.0 CZ N:TYR447 3.4 19.1 0.5 CE2 N:TYR408 3.8 17.7 1.0 CE1 N:TYR408 3.8 18.9 1.0 CE1 N:TYR447 3.9 20.0 0.5 O N:HOH785 4.0 17.0 1.0 O N:HOH38 4.1 15.0 1.0 C5 N:CAQ1 4.1 28.3 1.0 ND1 N:HIS460 4.1 16.2 1.0 ND1 N:HIS462 4.2 16.0 1.0 NH1 N:ARG457 4.2 17.0 1.0 O B:HOH209 4.2 19.1 1.0 CG N:HIS462 4.3 15.4 1.0 C2 N:CAQ1 4.3 29.5 1.0 CG N:HIS460 4.3 14.3 1.0 CE2 N:TYR447 4.5 20.6 0.5 OE1 N:GLN477 4.8 17.6 1.0

Iron binding site 3 out of 3 in the Axial Ligand Swapping in Double Mutant Maintains Intradiol-Cleavage Chemistry in Protocatechuate 3,4-Dioxygenase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Axial Ligand Swapping in Double Mutant Maintains Intradiol-Cleavage Chemistry in Protocatechuate 3,4-Dioxygenase within 5.0Å range: probe atom residue distance (Å) B Occ O:Fe600 b:18.9 occ:0.70 OH O:TYR408 1.9 23.3 1.0 NE2 O:HIS460 2.1 15.3 1.0 OH O:TYR447 2.1 17.6 0.5 NE2 O:HIS462 2.1 17.1 1.0 O3 O:CAQ1 2.2 24.4 1.0 O4 O:CAQ1 2.4 31.1 1.0 CE1 O:HIS460 2.9 16.2 1.0 C3 O:CAQ1 3.0 28.9 1.0 CE1 O:HIS462 3.0 17.1 1.0 CZ O:TYR408 3.0 22.0 1.0 C4 O:CAQ1 3.1 28.0 1.0 CD2 O:HIS462 3.2 17.0 1.0 CD2 O:HIS460 3.2 17.7 1.0 CZ O:TYR447 3.3 17.8 0.5 CE2 O:TYR408 3.8 20.3 1.0 CE1 O:TYR447 3.8 17.6 0.5 CE1 O:TYR408 3.9 22.4 1.0 O O:HOH787 4.0 16.9 1.0 ND1 O:HIS460 4.1 16.0 1.0 ND1 O:HIS462 4.2 16.6 1.0 O O:HOH121 4.2 15.8 1.0 NH1 O:ARG457 4.2 16.1 1.0 CG O:HIS460 4.3 15.3 1.0 C2 O:CAQ1 4.3 28.3 1.0 CG O:HIS462 4.3 15.6 1.0 O C:HOH207 4.3 20.5 1.0 C5 O:CAQ1 4.4 30.2 1.0 CE2 O:TYR447 4.4 18.6 0.5 OE1 O:GLN477 4.8 18.1 1.0

V.M.Purpero, J.D.Lipscomb. Axial Ligand Swapping in Double Mutant Maintains Intradiol-Cleavage Chemistry in Protocatechuate 3,4-Dioxygenase To Be Published.