Iron in PDB 4m27: Crystal Structure of Non-Heme Iron Oxygenase Orfp in Complex with Fe and L-Arg

The structure of Crystal Structure of Non-Heme Iron Oxygenase Orfp in Complex with Fe and L-Arg, PDB code: 4m27 was solved by C.Y.Chang, Y.C.Liu, S.Y.Lyu, C.C.Wu, T.L.Li, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 2.35
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	68.584, 117.005, 96.312, 90.00, 92.18, 90.00
R / Rfree (%)	20.3 / 27

The binding sites of Iron atom in the Crystal Structure of Non-Heme Iron Oxygenase Orfp in Complex with Fe and L-Arg (pdb code 4m27). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Crystal Structure of Non-Heme Iron Oxygenase Orfp in Complex with Fe and L-Arg, PDB code: 4m27:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the Crystal Structure of Non-Heme Iron Oxygenase Orfp in Complex with Fe and L-Arg


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 Non-Heme Iron Oxygenase Orfp in Complex with Fe and L-Arg within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe401 b:37.4 occ:1.00 OE1 A:GLU156 2.2 27.9 1.0 CE1 A:HIS154 2.5 30.0 1.0 NE2 A:HIS303 2.5 27.4 1.0 NE2 A:HIS154 3.1 29.9 1.0 CD A:GLU156 3.2 27.6 1.0 CD2 A:HIS303 3.3 27.6 1.0 OE2 A:GLU156 3.4 28.6 1.0 CE1 A:HIS303 3.5 27.6 1.0 ND1 A:HIS154 3.7 30.1 1.0 CD2 A:HIS154 4.4 29.9 1.0 NH2 A:ARG321 4.4 26.3 1.0 O A:HOH621 4.5 29.2 1.0 CG A:GLU156 4.5 26.6 1.0 CG A:HIS303 4.5 27.6 1.0 ND1 A:HIS303 4.6 27.4 1.0 CG A:HIS154 4.7 29.5 1.0 CB A:GLU156 4.9 25.8 1.0 CA A:GLU156 5.0 24.6 1.0

Iron binding site 2 out of 4 in the Crystal Structure of Non-Heme Iron Oxygenase Orfp in Complex with Fe and L-Arg


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 Non-Heme Iron Oxygenase Orfp in Complex with Fe and L-Arg within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe401 b:38.7 occ:1.00 NE2 B:HIS154 2.3 27.8 1.0 OE1 B:GLU156 2.3 26.7 1.0 NE2 B:HIS303 2.4 23.9 1.0 O B:HOH609 2.8 38.5 1.0 CE1 B:HIS154 3.0 27.4 1.0 CD2 B:HIS303 3.2 24.0 1.0 CD B:GLU156 3.3 27.3 1.0 CE1 B:HIS303 3.3 23.9 1.0 CD2 B:HIS154 3.4 27.3 1.0 OE2 B:GLU156 3.4 27.9 1.0 NH2 B:ARG321 3.5 35.0 1.0 ND1 B:HIS154 4.2 27.1 1.0 CG B:HIS303 4.4 23.7 1.0 ND1 B:HIS303 4.4 23.8 1.0 CG B:HIS154 4.5 27.1 1.0 O B:HOH591 4.5 23.7 1.0 CG B:GLU156 4.7 26.4 1.0 CZ B:ARG321 4.7 35.0 1.0

Iron binding site 3 out of 4 in the Crystal Structure of Non-Heme Iron Oxygenase Orfp in Complex with Fe and L-Arg


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 Non-Heme Iron Oxygenase Orfp in Complex with Fe and L-Arg within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe402 b:23.8 occ:1.00 NE2 C:HIS303 1.9 17.2 1.0 OE1 C:GLU156 2.2 18.1 1.0 NE2 C:HIS154 2.2 21.3 1.0 O3 C:SIN403 2.5 26.0 1.0 O4 C:SIN403 2.6 26.3 1.0 C4 C:SIN403 2.8 25.7 1.0 CE1 C:HIS303 2.9 17.1 1.0 CD2 C:HIS303 2.9 17.2 1.0 CE1 C:HIS154 3.0 21.2 1.0 CD C:GLU156 3.2 18.1 1.0 CB C:ARG401 3.3 33.5 1.0 CD2 C:HIS154 3.3 20.9 1.0 OE2 C:GLU156 3.5 18.6 1.0 CG C:ARG401 3.8 33.5 1.0 ND1 C:HIS303 4.0 16.9 1.0 CG C:HIS303 4.1 17.0 1.0 ND1 C:HIS154 4.2 21.0 1.0 NH2 C:ARG321 4.2 23.4 1.0 C3 C:SIN403 4.3 25.2 1.0 CG C:HIS154 4.4 20.6 1.0 CG C:GLU156 4.5 17.7 1.0 CA C:ARG401 4.6 34.1 1.0 N C:ARG401 4.8 33.4 1.0 CD2 C:LEU167 4.8 16.1 1.0 CZ C:ARG321 4.8 23.0 1.0 CB C:GLU156 4.9 17.5 1.0 NE C:ARG321 4.9 23.1 1.0 O C:ARG401 5.0 34.9 1.0

Iron binding site 4 out of 4 in the Crystal Structure of Non-Heme Iron Oxygenase Orfp in Complex with Fe and L-Arg


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 Non-Heme Iron Oxygenase Orfp in Complex with Fe and L-Arg within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe402 b:24.5 occ:1.00 O4 D:SIN403 1.9 33.2 1.0 OE1 D:GLU156 2.1 18.7 1.0 NE2 D:HIS154 2.2 19.2 1.0 NE2 D:HIS303 2.3 18.9 1.0 C4 D:SIN403 2.6 34.9 1.0 O3 D:SIN403 2.6 37.0 1.0 CD D:GLU156 3.0 18.8 1.0 CE1 D:HIS154 3.1 19.6 1.0 CD2 D:HIS303 3.2 18.8 1.0 CD2 D:HIS154 3.3 19.4 1.0 CE1 D:HIS303 3.3 18.8 1.0 OE2 D:GLU156 3.3 18.6 1.0 CB D:ARG401 3.4 34.2 1.0 CG D:ARG401 3.8 33.8 1.0 C3 D:SIN403 4.0 34.0 1.0 ND1 D:HIS154 4.3 19.5 1.0 ND1 D:HIS303 4.4 18.8 1.0 CG D:HIS303 4.4 19.1 1.0 CG D:HIS154 4.4 19.5 1.0 CG D:GLU156 4.4 19.0 1.0 CA D:ARG401 4.6 34.7 1.0 N D:ARG401 4.7 34.8 1.0 CB D:GLU156 4.8 19.4 1.0 C2 D:SIN403 4.8 33.1 1.0 NH2 D:ARG321 4.8 30.2 1.0 CA D:GLU156 4.9 19.6 1.0

C.Y.Chang, S.Y.Lyu, Y.C.Liu, N.S.Hsu, C.C.Wu, C.F.Tang, K.H.Lin, J.Y.Ho, C.J.Wu, M.D.Tsai, T.L.Li. Biosynthesis of Streptolidine Involved Two Unexpected Intermediates Produced By A Dihydroxylase and A Cyclase Through Unusual Mechanisms. Angew.Chem.Int.Ed.Engl. V. 53 1943 2014.
ISSN: ISSN 1433-7851
PubMed: 24505011
DOI: 10.1002/ANIE.201307989