Iron in PDB 4m2e: Crystal Structure of Non-Heme Iron Oxygenase Orfp in Complex with Fe and L-Homoarginine

The structure of Crystal Structure of Non-Heme Iron Oxygenase Orfp in Complex with Fe and L-Homoarginine, PDB code: 4m2e 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 / 2.06
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	68.322, 117.162, 96.038, 90.00, 91.62, 90.00
R / Rfree (%)	22.3 / 28.8

The binding sites of Iron atom in the Crystal Structure of Non-Heme Iron Oxygenase Orfp in Complex with Fe and L-Homoarginine (pdb code 4m2e). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 3 binding sites of Iron where determined in the Crystal Structure of Non-Heme Iron Oxygenase Orfp in Complex with Fe and L-Homoarginine, PDB code: 4m2e:
Jump to Iron binding site number: 1; 2; 3;

Iron binding site 1 out of 3 in the Crystal Structure of Non-Heme Iron Oxygenase Orfp in Complex with Fe and L-Homoarginine


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-Homoarginine within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe401 b:89.3 occ:1.00 OE1 B:GLU156 2.5 46.0 1.0 NE2 B:HIS303 2.6 36.9 1.0 NE2 B:HIS154 2.6 37.7 1.0 CE1 B:HIS154 3.0 36.3 1.0 CE1 B:HIS303 3.1 37.5 1.0 CD2 B:HIS303 3.5 36.6 1.0 O B:HOH652 3.6 44.4 1.0 CD2 B:HIS154 3.7 36.9 1.0 CD B:GLU156 3.7 44.2 1.0 ND1 B:HIS303 4.1 35.9 1.0 ND1 B:HIS154 4.2 36.4 1.0 OE2 B:GLU156 4.3 45.3 1.0 CG B:HIS303 4.4 35.5 1.0 CG B:HIS154 4.5 35.3 1.0 NH2 B:ARG321 4.6 45.0 1.0 CB B:GLU156 4.9 36.6 1.0 CG B:GLU156 4.9 39.5 1.0

Iron binding site 2 out of 3 in the Crystal Structure of Non-Heme Iron Oxygenase Orfp in Complex with Fe and L-Homoarginine


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-Homoarginine within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe401 b:68.0 occ:1.00 OE1 C:GLU156 2.3 24.4 1.0 NE2 C:HIS154 2.6 22.7 1.0 NE2 C:HIS303 2.6 19.7 1.0 CE1 C:HIS154 3.0 22.2 1.0 CD C:GLU156 3.2 23.9 1.0 CE1 C:HIS303 3.3 19.2 1.0 CB C:HRG402 3.3 34.0 1.0 O C:HOH657 3.4 37.4 1.0 OE2 C:GLU156 3.4 25.5 1.0 O C:HOH664 3.4 47.5 1.0 CD2 C:HIS303 3.6 19.0 1.0 CD2 C:HIS154 3.8 21.7 1.0 NH2 C:ARG321 3.9 23.3 1.0 CG' C:HRG402 3.9 34.0 1.0 CG C:HRG402 4.2 33.5 1.0 ND1 C:HIS154 4.3 22.6 1.0 ND1 C:HIS303 4.4 18.9 1.0 CD2 C:LEU151 4.5 32.1 1.0 CG C:HIS303 4.6 19.1 1.0 CG C:GLU156 4.6 22.8 1.0 CA C:HRG402 4.7 33.4 1.0 CG C:HIS154 4.7 21.8 1.0 O C:HOH672 4.8 32.5 1.0 CZ C:ARG321 4.8 23.1 1.0 N C:HRG402 4.9 32.2 1.0 O C:HRG402 4.9 34.5 1.0 CB C:GLU156 5.0 20.8 1.0

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


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-Homoarginine within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe401 b:70.5 occ:1.00 OE1 D:GLU156 2.3 26.0 1.0 NE2 D:HIS303 2.7 27.1 1.0 NE2 D:HIS154 2.8 23.7 1.0 CE1 D:HIS154 3.1 24.4 1.0 CD D:GLU156 3.2 25.7 1.0 CE1 D:HIS303 3.3 27.2 1.0 OE2 D:GLU156 3.4 26.1 1.0 CB D:HRG402 3.6 35.2 1.0 CD2 D:HIS303 3.7 26.9 1.0 CD2 D:HIS154 4.1 23.7 1.0 CG D:HRG402 4.3 34.9 1.0 ND1 D:HIS303 4.4 27.4 1.0 ND1 D:HIS154 4.4 24.1 1.0 CG' D:HRG402 4.5 36.2 1.0 CD2 D:LEU151 4.6 34.8 1.0 CG D:GLU156 4.6 24.5 1.0 CG D:HIS303 4.6 26.8 1.0 CA D:HRG402 4.7 35.4 1.0 N D:HRG402 4.8 33.1 1.0 O D:HOH519 4.9 25.0 1.0 CG D:HIS154 4.9 23.2 1.0 CB D:GLU156 5.0 22.8 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