Iron in PDB 3gte: Crystal Structure of Dicamba Monooxygenase with Non-Heme Iron

The structure of Crystal Structure of Dicamba Monooxygenase with Non-Heme Iron, PDB code: 3gte was solved by T.J.Rydel, E.J.Sturman, F.Moshiri, G.R.Brown, Y.Qi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 1.95
Space group	P 32
Cell size a, b, c (Å), α, β, γ (°)	81.110, 81.110, 158.810, 90.00, 90.00, 120.00
R / Rfree (%)	n/a / n/a

The binding sites of Iron atom in the Crystal Structure of Dicamba Monooxygenase with Non-Heme Iron (pdb code 3gte). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 8 binding sites of Iron where determined in the Crystal Structure of Dicamba Monooxygenase with Non-Heme Iron, PDB code: 3gte:
Jump to Iron binding site number: 1; 2; 3; 4; 5; 6; 7; 8;

Iron binding site 1 out of 8 in the Crystal Structure of Dicamba Monooxygenase with Non-Heme Iron


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structure of Dicamba Monooxygenase with Non-Heme Iron within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:24.2 occ:1.00 FE1 A:FES501 0.0 24.2 1.0 S1 A:FES501 2.2 26.0 1.0 S2 A:FES501 2.2 25.5 1.0 SG A:CYS68 2.3 23.2 1.0 SG A:CYS49 2.4 24.3 1.0 FE2 A:FES501 2.7 26.0 1.0 CB A:CYS49 3.1 25.4 1.0 CB A:CYS68 3.2 18.7 1.0 CB A:HIS51 4.1 25.5 1.0 CB A:TYR70 4.1 28.4 1.0 N A:HIS71 4.3 29.0 1.0 CB A:ALA54 4.5 27.4 1.0 ND1 A:HIS71 4.6 27.6 1.0 ND1 A:HIS51 4.6 27.1 1.0 CA A:CYS49 4.6 26.1 1.0 CA A:CYS68 4.6 22.8 1.0 N A:ARG52 4.7 28.9 1.0 CG A:HIS51 4.9 28.6 1.0 N A:TYR70 4.9 27.2 1.0 CD1 A:LEU73 4.9 29.8 1.0 CA A:TYR70 4.9 28.5 1.0 CG A:LEU73 5.0 28.1 1.0

Iron binding site 2 out of 8 in the Crystal Structure of Dicamba Monooxygenase with Non-Heme Iron


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Crystal Structure of Dicamba Monooxygenase with Non-Heme Iron within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:26.0 occ:1.00 FE2 A:FES501 0.0 26.0 1.0 ND1 A:HIS71 2.2 27.6 1.0 S1 A:FES501 2.2 26.0 1.0 S2 A:FES501 2.3 25.5 1.0 ND1 A:HIS51 2.3 27.1 1.0 FE1 A:FES501 2.7 24.2 1.0 CG A:HIS71 3.1 30.0 1.0 CE1 A:HIS71 3.2 30.8 1.0 CG A:HIS51 3.3 28.6 1.0 CB A:HIS71 3.3 30.1 1.0 CE1 A:HIS51 3.3 27.6 1.0 CB A:HIS51 3.5 25.5 1.0 N A:HIS71 3.7 29.0 1.0 CB A:TYR70 4.0 28.4 1.0 CA A:HIS71 4.1 29.4 1.0 CD2 A:HIS71 4.2 31.7 1.0 N A:ARG52 4.2 28.9 1.0 NE2 A:HIS71 4.3 30.4 1.0 CG A:TYR70 4.4 30.1 1.0 CD1 A:TYR70 4.4 29.5 1.0 CD2 A:HIS51 4.4 24.6 1.0 NE2 A:HIS51 4.4 27.7 1.0 SG A:CYS68 4.5 23.2 1.0 SG A:CYS49 4.5 24.3 1.0 C A:TYR70 4.5 29.2 1.0 CB A:ARG52 4.6 29.1 1.0 CA A:HIS51 4.8 28.0 1.0 CA A:TYR70 4.9 28.5 1.0 C A:HIS51 4.9 29.7 1.0 C A:HIS71 4.9 30.3 1.0 CG A:ARG52 5.0 32.4 1.0

Iron binding site 3 out of 8 in the Crystal Structure of Dicamba Monooxygenase with Non-Heme Iron


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Crystal Structure of Dicamba Monooxygenase with Non-Heme Iron within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe502 b:39.7 occ:1.00 O A:ACT650 2.1 38.6 1.0 NE2 A:HIS165 2.1 47.0 1.0 NE2 A:HIS160 2.3 42.6 1.0 OD2 A:ASP294 2.3 43.3 1.0 OD1 A:ASP294 2.5 42.1 1.0 OXT A:ACT650 2.7 38.7 1.0 CG A:ASP294 2.8 40.6 1.0 C A:ACT650 2.8 40.1 1.0 CE1 A:HIS165 3.0 46.3 1.0 CD2 A:HIS165 3.2 46.1 1.0 CD2 A:HIS160 3.3 42.7 1.0 CE1 A:HIS160 3.3 42.6 1.0 OD1 A:ASN154 3.6 37.1 1.0 O A:HOH734 4.0 35.5 1.0 ND1 A:HIS165 4.2 46.0 1.0 CD1 A:LEU290 4.2 49.5 1.0 CH3 A:ACT650 4.3 37.8 1.0 CB A:ASP294 4.3 40.0 1.0 CG A:HIS165 4.3 46.4 1.0 ND1 A:HIS160 4.4 41.5 1.0 CG A:HIS160 4.4 42.6 1.0 ND2 A:ASN154 4.5 39.7 1.0 CG A:ASN154 4.5 36.7 1.0 O A:ALA289 4.5 45.8 1.0

Iron binding site 4 out of 8 in the Crystal Structure of Dicamba Monooxygenase with Non-Heme Iron


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Crystal Structure of Dicamba Monooxygenase with Non-Heme Iron within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe501 b:31.5 occ:1.00 FE1 B:FES501 0.0 31.5 1.0 S1 B:FES501 2.2 31.8 1.0 S2 B:FES501 2.3 30.1 1.0 SG B:CYS49 2.3 34.2 1.0 SG B:CYS68 2.4 31.9 1.0 FE2 B:FES501 2.7 31.8 1.0 CB B:CYS49 3.1 31.3 1.0 CB B:CYS68 3.3 33.1 1.0 CB B:HIS51 4.0 31.1 1.0 CB B:TYR70 4.2 31.9 1.0 N B:HIS71 4.4 33.7 1.0 ND1 B:HIS51 4.5 31.4 1.0 CB B:ALA54 4.5 29.0 1.0 ND1 B:HIS71 4.6 37.5 1.0 CA B:CYS49 4.6 31.5 1.0 N B:ARG52 4.7 31.7 1.0 CA B:CYS68 4.7 31.6 1.0 CG B:HIS51 4.8 30.8 1.0 CD1 B:LEU73 4.8 33.2 1.0 N B:HIS51 4.9 29.2 1.0 N B:TYR70 4.9 32.4 1.0 CG B:LEU73 4.9 34.9 1.0 CB B:LEU73 5.0 33.1 1.0 CA B:TYR70 5.0 32.0 1.0

Iron binding site 5 out of 8 in the Crystal Structure of Dicamba Monooxygenase with Non-Heme Iron


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 5 of Crystal Structure of Dicamba Monooxygenase with Non-Heme Iron within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe501 b:31.8 occ:1.00 FE2 B:FES501 0.0 31.8 1.0 ND1 B:HIS51 2.2 31.4 1.0 S1 B:FES501 2.2 31.8 1.0 ND1 B:HIS71 2.2 37.5 1.0 S2 B:FES501 2.3 30.1 1.0 FE1 B:FES501 2.7 31.5 1.0 CG B:HIS71 3.1 36.5 1.0 CG B:HIS51 3.1 30.8 1.0 CE1 B:HIS71 3.2 37.8 1.0 CE1 B:HIS51 3.2 33.3 1.0 CB B:HIS71 3.3 35.4 1.0 CB B:HIS51 3.3 31.1 1.0 N B:HIS71 3.8 33.7 1.0 CB B:TYR70 4.0 31.9 1.0 CA B:HIS71 4.2 34.1 1.0 N B:ARG52 4.2 31.7 1.0 CD2 B:HIS71 4.2 37.2 1.0 NE2 B:HIS71 4.3 37.6 1.0 CD2 B:HIS51 4.3 30.7 1.0 NE2 B:HIS51 4.3 29.9 1.0 SG B:CYS49 4.4 34.2 1.0 CD1 B:TYR70 4.4 33.4 1.0 CG B:TYR70 4.4 33.2 1.0 CB B:ARG52 4.5 32.2 1.0 SG B:CYS68 4.5 31.9 1.0 C B:TYR70 4.6 33.4 1.0 CA B:HIS51 4.6 31.0 1.0 C B:HIS51 4.8 32.0 1.0 CG B:ARG52 4.9 35.4 1.0 CA B:ARG52 4.9 31.4 1.0 CA B:TYR70 5.0 32.0 1.0

Iron binding site 6 out of 8 in the Crystal Structure of Dicamba Monooxygenase with Non-Heme Iron


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 6 of Crystal Structure of Dicamba Monooxygenase with Non-Heme Iron within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe502 b:31.9 occ:1.00 OD2 B:ASP294 2.1 35.4 1.0 NE2 B:HIS165 2.1 26.8 1.0 O B:ACT652 2.2 35.1 1.0 NE2 B:HIS160 2.3 35.1 1.0 OD1 B:ASP294 2.6 35.2 1.0 CG B:ASP294 2.7 32.7 1.0 CD2 B:HIS165 3.0 27.1 1.0 C B:ACT652 3.1 35.1 1.0 CE1 B:HIS165 3.2 27.4 1.0 CD2 B:HIS160 3.2 35.3 1.0 OXT B:ACT652 3.2 36.3 1.0 CE1 B:HIS160 3.3 35.6 1.0 OD1 B:ASN154 3.6 34.5 1.0 O B:HOH892 4.1 37.5 1.0 CB B:ASP294 4.1 33.9 1.0 CG B:HIS165 4.2 27.4 1.0 ND1 B:HIS165 4.2 23.8 1.0 ND1 B:HIS160 4.3 33.9 1.0 CG B:HIS160 4.4 34.5 1.0 CD1 B:LEU290 4.4 41.5 1.0 ND2 B:ASN154 4.4 33.5 1.0 CG B:ASN154 4.4 33.7 1.0 CH3 B:ACT652 4.5 34.4 1.0 O B:ALA289 4.8 36.0 1.0

Iron binding site 7 out of 8 in the Crystal Structure of Dicamba Monooxygenase with Non-Heme Iron


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 7 of Crystal Structure of Dicamba Monooxygenase with Non-Heme Iron within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe501 b:26.4 occ:1.00 FE1 C:FES501 0.0 26.4 1.0 S1 C:FES501 2.2 29.6 1.0 S2 C:FES501 2.2 27.6 1.0 SG C:CYS68 2.3 29.1 1.0 SG C:CYS49 2.4 23.5 1.0 FE2 C:FES501 2.7 27.5 1.0 CB C:CYS49 3.1 25.2 1.0 CB C:CYS68 3.2 25.1 1.0 CB C:HIS51 4.0 25.1 1.0 CB C:TYR70 4.3 28.5 1.0 N C:HIS71 4.4 29.7 1.0 ND1 C:HIS51 4.5 27.5 1.0 CA C:CYS49 4.5 27.5 1.0 CB C:ALA54 4.5 26.5 1.0 ND1 C:HIS71 4.6 27.8 1.0 N C:ARG52 4.7 26.8 1.0 CA C:CYS68 4.7 26.2 1.0 CG C:HIS51 4.7 28.1 1.0 CD1 C:LEU73 4.8 26.0 1.0 N C:HIS51 4.9 25.1 1.0 CG C:LEU73 4.9 28.6 1.0 CB C:LEU73 4.9 27.9 1.0 CA C:HIS51 5.0 26.9 1.0 N C:TYR70 5.0 28.0 1.0

Iron binding site 8 out of 8 in the Crystal Structure of Dicamba Monooxygenase with Non-Heme Iron


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 8 of Crystal Structure of Dicamba Monooxygenase with Non-Heme Iron within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe501 b:27.5 occ:1.00 FE2 C:FES501 0.0 27.5 1.0 ND1 C:HIS51 2.2 27.5 1.0 S1 C:FES501 2.2 29.6 1.0 S2 C:FES501 2.3 27.6 1.0 ND1 C:HIS71 2.3 27.8 1.0 FE1 C:FES501 2.7 26.4 1.0 CG C:HIS51 3.1 28.1 1.0 CG C:HIS71 3.1 30.3 1.0 CE1 C:HIS71 3.3 30.2 1.0 CE1 C:HIS51 3.3 26.7 1.0 CB C:HIS51 3.3 25.1 1.0 CB C:HIS71 3.4 27.6 1.0 N C:HIS71 3.8 29.7 1.0 CB C:TYR70 4.0 28.5 1.0 N C:ARG52 4.1 26.8 1.0 CA C:HIS71 4.2 29.1 1.0 CD2 C:HIS71 4.3 30.0 1.0 CD2 C:HIS51 4.3 26.7 1.0 NE2 C:HIS71 4.3 28.2 1.0 NE2 C:HIS51 4.3 27.9 1.0 CD1 C:TYR70 4.4 28.7 1.0 CG C:TYR70 4.4 28.8 1.0 CB C:ARG52 4.4 28.7 1.0 SG C:CYS68 4.5 29.1 1.0 SG C:CYS49 4.6 23.5 1.0 CA C:HIS51 4.6 26.9 1.0 C C:TYR70 4.6 30.1 1.0 C C:HIS51 4.8 27.6 1.0 CA C:ARG52 4.9 28.3 1.0 CG C:ARG52 4.9 32.5 1.0 CA C:TYR70 4.9 29.1 1.0 CD C:ARG52 5.0 37.0 1.0

R.L.D'ordine, T.J.Rydel, M.J.Storek, E.J.Sturman, F.Moshiri, R.K.Bartlett, G.R.Brown, R.J.Eilers, C.Dart, Y.Qi, S.Flasinski, S.J.Franklin. Dicamba Monooxygenase: Structural Insights Into A Dynamic Rieske Oxygenase That Catalyzes An Exocyclic Monooxygenation. J.Mol.Biol. V. 392 481 2009.
ISSN: ISSN 0022-2836
PubMed: 19616009
DOI: 10.1016/J.JMB.2009.07.022