Iron in PDB 1wql: Cumene Dioxygenase (CUMA1A2) From Pseudomonas Fluorescens IP01

The structure of Cumene Dioxygenase (CUMA1A2) From Pseudomonas Fluorescens IP01, PDB code: 1wql was solved by X.Dong, S.Fushinobu, E.Fukuda, T.Terada, S.Nakamura, K.Shimizu, H.Nojiri, T.Omori, H.Shoun, T.Wakagi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.65 / 2.20
Space group	P 21 3
Cell size a, b, c (Å), α, β, γ (°)	147.036, 147.036, 147.036, 90.00, 90.00, 90.00
R / Rfree (%)	17.3 / 19.6

The binding sites of Iron atom in the Cumene Dioxygenase (CUMA1A2) From Pseudomonas Fluorescens IP01 (pdb code 1wql). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 3 binding sites of Iron where determined in the Cumene Dioxygenase (CUMA1A2) From Pseudomonas Fluorescens IP01, PDB code: 1wql:
Jump to Iron binding site number: 1; 2; 3;

Iron binding site 1 out of 3 in the Cumene Dioxygenase (CUMA1A2) From Pseudomonas Fluorescens IP01


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Cumene Dioxygenase (CUMA1A2) From Pseudomonas Fluorescens IP01 within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe502 b:15.3 occ:1.00 OD2 A:ASP388 2.0 16.2 1.0 NE2 A:HIS240 2.0 14.3 1.0 O1 A:OXY503 2.1 25.9 1.0 NE2 A:HIS234 2.1 16.5 1.0 O2 A:OXY503 2.7 29.3 1.0 CG A:ASP388 2.8 22.7 1.0 CE1 A:HIS240 2.9 15.8 1.0 OD1 A:ASP388 2.9 22.2 1.0 CD2 A:HIS234 3.1 14.1 1.0 CD2 A:HIS240 3.1 16.4 1.0 CE1 A:HIS234 3.2 14.9 1.0 NE2 A:GLN227 3.4 18.2 1.0 ND1 A:HIS240 4.0 15.4 1.0 CG A:HIS240 4.2 18.1 1.0 CB A:ASP388 4.2 19.2 1.0 CG A:HIS234 4.3 15.3 1.0 ND1 A:HIS234 4.3 15.1 1.0 CD A:GLN227 4.6 17.1 1.0 CE1 A:PHE378 4.6 15.6 1.0 CA A:ASP388 4.8 19.2 1.0 CZ A:PHE378 4.9 11.9 1.0

Iron binding site 2 out of 3 in the Cumene Dioxygenase (CUMA1A2) From Pseudomonas Fluorescens IP01


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Cumene Dioxygenase (CUMA1A2) From Pseudomonas Fluorescens IP01 within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:15.9 occ:1.00 FE1 A:FES501 0.0 15.9 1.0 ND1 A:HIS124 2.2 16.8 1.0 ND1 A:HIS103 2.2 17.0 1.0 S1 A:FES501 2.2 17.0 1.0 S2 A:FES501 2.2 17.4 1.0 FE2 A:FES501 2.7 15.6 1.0 CG A:HIS124 3.0 16.1 1.0 CG A:HIS103 3.1 18.5 1.0 CE1 A:HIS124 3.2 14.8 1.0 CE1 A:HIS103 3.2 19.3 1.0 CB A:HIS124 3.3 14.2 1.0 CB A:HIS103 3.3 17.4 1.0 N A:HIS124 3.8 16.9 1.0 CB A:TYR123 4.0 14.8 1.0 CA A:HIS124 4.1 17.6 1.0 CD2 A:HIS124 4.2 15.3 1.0 NE2 A:HIS124 4.2 15.0 1.0 CG A:TYR123 4.3 14.2 1.0 CD2 A:HIS103 4.3 17.3 1.0 CD2 A:TYR123 4.3 13.8 1.0 NE2 A:HIS103 4.3 18.1 1.0 N A:ARG104 4.4 17.1 1.0 SG A:CYS101 4.5 15.9 1.0 SG A:CYS121 4.5 15.6 1.0 C A:TYR123 4.5 19.6 1.0 CB A:ARG104 4.6 18.0 1.0 CA A:HIS103 4.6 16.9 1.0 C A:HIS103 4.8 15.1 1.0 CA A:TYR123 4.9 16.4 1.0 CG A:ARG104 4.9 15.5 1.0 C A:HIS124 5.0 18.1 1.0 CD1 A:TRP126 5.0 16.1 1.0

Iron binding site 3 out of 3 in the Cumene Dioxygenase (CUMA1A2) From Pseudomonas Fluorescens IP01


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Cumene Dioxygenase (CUMA1A2) From Pseudomonas Fluorescens IP01 within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:15.6 occ:1.00 FE2 A:FES501 0.0 15.6 1.0 S1 A:FES501 2.2 17.0 1.0 S2 A:FES501 2.2 17.4 1.0 SG A:CYS121 2.3 15.6 1.0 SG A:CYS101 2.4 15.9 1.0 FE1 A:FES501 2.7 15.9 1.0 CB A:CYS101 3.1 14.4 1.0 CB A:CYS121 3.2 16.2 1.0 CB A:HIS103 4.1 17.4 1.0 CB A:TYR123 4.2 14.8 1.0 CB A:MET106 4.3 16.8 1.0 CB A:TRP126 4.5 16.9 1.0 N A:HIS124 4.5 16.9 1.0 ND1 A:HIS103 4.5 17.0 1.0 ND1 A:HIS124 4.6 16.8 1.0 CA A:CYS101 4.6 17.0 1.0 CA A:CYS121 4.6 18.1 1.0 CG A:TRP126 4.7 15.8 1.0 CG A:HIS103 4.8 18.5 1.0 N A:ARG104 4.9 17.1 1.0 C A:CYS121 4.9 19.8 1.0 O A:CYS121 4.9 18.0 1.0

X.Dong, S.Fushinobu, E.Fukuda, T.Terada, S.Nakamura, K.Shimizu, H.Nojiri, T.Omori, H.Shoun, T.Wakagi. Crystal Structure of the Terminal Oxygenase Component of Cumene Dioxygenase From Pseudomonas Fluorescens IP01 J.Bacteriol. V. 187 2483 2005.
ISSN: ISSN 0021-9193
PubMed: 15774891
DOI: 10.1128/JB.187.7.2483-2490.2005