Iron in PDB 3mv4: 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: 3mv4 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)	30.60 / 1.59
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	128.311, 140.487, 168.061, 90.00, 90.00, 90.00
R / Rfree (%)	14.6 / 16.7

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 3mv4). 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: 3mv4:
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:21.9 occ:0.60 OH M:TYR408 2.0 18.1 1.0 OH M:TYR462 2.1 21.2 1.0 O2 M:CO3543 2.1 21.6 0.6 NE2 M:HIS460 2.2 17.2 1.0 O1 M:CO3543 2.3 20.8 0.6 C M:CO3543 2.5 22.0 0.6 NE2 M:HIS447 2.9 11.8 0.5 CE1 M:HIS460 3.0 15.8 1.0 CZ M:TYR408 3.0 14.7 1.0 CZ M:TYR462 3.0 15.6 1.0 CE2 M:TYR462 3.2 16.0 1.0 CD2 M:HIS460 3.4 15.8 1.0 CE1 M:HIS447 3.6 14.0 0.5 CE2 M:TYR408 3.6 16.1 1.0 O3 M:CO3543 3.8 22.9 0.6 CE1 M:TYR408 4.0 13.7 1.0 CD2 M:HIS447 4.1 14.4 0.5 NH1 M:ARG457 4.1 15.6 1.0 O M:HOH220 4.1 19.2 1.0 ND1 M:HIS460 4.2 14.2 1.0 CE1 M:TYR462 4.3 13.5 1.0 O M:HOH151 4.4 15.0 1.0 CG M:HIS460 4.4 14.9 1.0 CD2 M:TYR462 4.6 14.3 1.0 CG M:ARG457 4.7 14.4 1.0 ND1 M:HIS447 4.8 22.6 0.5 ND1 M:HIS447 4.8 14.0 0.5 CD2 A:TYR16 4.9 20.7 1.0 O A:HOH211 4.9 17.4 1.0 CD2 M:TYR408 4.9 14.3 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:20.9 occ:0.60 OH N:TYR408 2.0 16.9 1.0 OH N:TYR462 2.1 22.6 1.0 O3 N:CO3542 2.1 23.9 0.6 O1 N:CO3542 2.2 23.2 0.6 NE2 N:HIS460 2.2 16.5 1.0 C N:CO3542 2.5 24.9 0.6 CE1 N:HIS460 2.9 16.3 1.0 NE2 N:HIS447 2.9 22.5 0.5 CZ N:TYR408 3.0 14.6 1.0 CZ N:TYR462 3.1 16.3 1.0 CE2 N:TYR462 3.2 15.3 1.0 CD2 N:HIS460 3.5 17.3 1.0 CE2 N:TYR408 3.6 14.8 1.0 CE1 N:HIS447 3.6 23.6 0.5 O2 N:CO3542 3.8 25.6 0.6 CE1 N:TYR408 4.0 14.9 1.0 O N:HOH82 4.0 18.3 1.0 CD2 N:HIS447 4.0 23.2 0.5 NH2 N:ARG457 4.0 14.9 1.0 ND1 N:HIS460 4.2 14.4 1.0 CE1 N:TYR462 4.4 13.1 1.0 O N:HOH207 4.4 15.3 1.0 CG N:HIS460 4.4 13.8 1.0 CD2 N:TYR462 4.6 13.7 1.0 CG N:ARG457 4.7 14.6 1.0 CD2 N:HIS447 4.7 23.2 0.5 O N:HOH1555 4.8 48.4 1.0 ND1 N:HIS447 4.9 20.2 0.5 CD2 N:TYR408 4.9 14.8 1.0 O B:HOH228 5.0 19.1 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:21.3 occ:0.60 OH O:TYR408 2.0 17.8 1.0 OH O:TYR462 2.1 22.9 1.0 O3 O:CO31 2.2 23.0 0.6 NE2 O:HIS460 2.2 16.4 1.0 O2 O:CO31 2.3 22.9 0.6 C O:CO31 2.6 23.7 0.6 CE1 O:HIS460 2.9 15.4 1.0 NE2 O:HIS447 3.0 12.6 0.5 CZ O:TYR408 3.0 15.0 1.0 CZ O:TYR462 3.1 16.1 1.0 CE2 O:TYR462 3.2 15.9 1.0 CD2 O:HIS460 3.4 16.6 1.0 CE1 O:HIS447 3.6 14.6 0.5 CE2 O:TYR408 3.7 15.2 1.0 O1 O:CO31 3.9 23.9 0.6 CE1 O:TYR408 4.0 15.5 1.0 NH1 O:ARG457 4.1 15.2 1.0 O O:HOH172 4.1 18.3 1.0 CD2 O:HIS447 4.1 15.3 0.5 ND1 O:HIS460 4.2 14.7 1.0 CE1 O:TYR462 4.3 13.4 1.0 O O:HOH135 4.4 15.4 1.0 CG O:HIS460 4.4 14.2 1.0 CD2 O:TYR462 4.5 13.9 1.0 CG O:ARG457 4.7 13.8 1.0 ND1 O:HIS447 4.8 16.3 0.5 ND1 O:HIS447 4.9 23.0 0.5 O C:HOH226 4.9 20.2 1.0 O O:HOH1563 4.9 40.4 1.0 CD2 O:TYR408 5.0 14.9 1.0 CD2 C:TYR16 5.0 24.1 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.