Iron in PDB 4m2i: Crystal Structure of Non-Heme Iron Oxygenase Orfp in Complex with Fe

The structure of Crystal Structure of Non-Heme Iron Oxygenase Orfp in Complex with Fe, PDB code: 4m2i 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 / 2.53
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	56.507, 115.527, 95.288, 90.00, 90.78, 90.00
R / Rfree (%)	19.7 / 26.7

The binding sites of Iron atom in the Crystal Structure of Non-Heme Iron Oxygenase Orfp in Complex with Fe (pdb code 4m2i). 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, PDB code: 4m2i:
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


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 within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe401 b:48.1 occ:1.00 NE2 A:HIS154 2.2 40.2 1.0 OE1 A:GLU156 2.2 41.1 1.0 NE2 A:HIS303 2.4 29.6 1.0 O A:HOH567 2.5 37.5 1.0 CE1 A:HIS154 2.8 39.9 1.0 O A:HOH566 3.0 34.3 1.0 CE1 A:HIS303 3.1 28.6 1.0 CD A:GLU156 3.4 42.4 1.0 CD2 A:HIS154 3.4 38.3 1.0 CD2 A:HIS303 3.5 28.9 1.0 NH2 A:ARG321 3.6 43.6 1.0 OE2 A:GLU156 3.9 46.3 1.0 ND1 A:HIS154 4.1 38.8 1.0 ND1 A:HIS303 4.3 28.8 1.0 CG A:HIS154 4.4 37.8 1.0 CG A:HIS303 4.5 28.8 1.0 CG A:GLU156 4.6 39.8 1.0 CB A:GLU156 4.8 38.1 1.0 CZ A:ARG321 4.8 41.8 1.0 CA A:GLU156 4.9 36.9 1.0

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


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 within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe401 b:63.3 occ:1.00 NE2 B:HIS303 2.4 29.0 1.0 OE1 B:GLU156 2.5 50.7 1.0 NE2 B:HIS154 2.7 42.4 1.0 CE1 B:HIS154 2.9 44.5 1.0 O B:HOH559 3.1 46.7 1.0 CE1 B:HIS303 3.3 29.9 1.0 CD B:GLU156 3.3 50.2 1.0 CD2 B:HIS303 3.4 29.1 1.0 OE2 B:GLU156 3.7 54.4 1.0 CD2 B:HIS154 3.9 41.4 1.0 ND1 B:HIS154 4.1 42.5 1.0 ND1 B:HIS303 4.4 30.2 1.0 CG B:GLU156 4.5 45.9 1.0 CG B:HIS303 4.5 29.6 1.0 CB B:GLU156 4.6 43.3 1.0 CG B:HIS154 4.6 40.2 1.0 NH1 B:ARG321 4.7 55.2 1.0 CA B:GLU156 4.8 40.6 1.0

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


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 within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe401 b:77.3 occ:1.00 NE2 C:HIS303 2.3 37.0 1.0 NE2 C:HIS154 2.5 49.6 1.0 OE1 C:GLU156 2.5 49.2 1.0 CE1 C:HIS154 2.9 51.3 1.0 CE1 C:HIS303 3.1 36.6 1.0 CD2 C:HIS303 3.3 37.3 1.0 CD C:GLU156 3.5 49.0 1.0 CD2 C:HIS154 3.7 48.0 1.0 NH2 C:ARG321 3.8 55.7 1.0 OE2 C:GLU156 3.9 52.1 1.0 ND1 C:HIS154 4.1 50.1 1.0 ND1 C:HIS303 4.3 37.3 1.0 CG C:HIS303 4.4 37.5 1.0 CG C:HIS154 4.5 48.1 1.0 CZ C:ARG321 4.6 55.1 1.0 NH1 C:ARG321 4.7 55.7 1.0 CD2 C:LEU151 4.7 75.3 1.0 CG C:GLU156 4.8 46.7 1.0 O C:HIS303 4.9 43.8 1.0

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


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 within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe401 b:80.3 occ:1.00 NE2 D:HIS303 2.5 43.2 1.0 OE1 D:GLU156 2.7 58.9 1.0 NE2 D:HIS154 2.8 61.1 1.0 CE1 D:HIS154 3.1 60.4 1.0 CE1 D:HIS303 3.3 42.6 1.0 CD2 D:HIS303 3.4 43.2 1.0 CD D:GLU156 3.8 58.6 1.0 CD2 D:HIS154 4.0 58.2 1.0 OE2 D:GLU156 4.2 61.0 1.0 ND1 D:HIS154 4.2 58.1 1.0 ND1 D:HIS303 4.4 42.0 1.0 CG D:HIS303 4.5 43.4 1.0 CG D:HIS154 4.7 56.3 1.0 O D:HIS303 4.9 48.0 1.0 CG D:GLU156 5.0 55.1 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