Iron in PDB 4m2c: Crystal Structure of Non-Heme Iron Oxygenase Orfp in Complex with Fe and D-Arg

The structure of Crystal Structure of Non-Heme Iron Oxygenase Orfp in Complex with Fe and D-Arg, PDB code: 4m2c 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 (°)	68.034, 116.369, 95.800, 90.00, 91.44, 90.00
R / Rfree (%)	22.3 / 27.6

The binding sites of Iron atom in the Crystal Structure of Non-Heme Iron Oxygenase Orfp in Complex with Fe and D-Arg (pdb code 4m2c). 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 D-Arg, PDB code: 4m2c:
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 D-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 D-Arg within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe401 b:94.4 occ:1.00 OE1 B:GLU156 2.7 47.4 1.0 CE1 B:HIS154 2.7 45.0 1.0 NE2 B:HIS154 2.8 45.4 1.0 NE2 B:HIS303 3.2 46.5 1.0 O B:HOH608 3.4 53.3 1.0 CE1 B:HIS303 3.4 46.8 1.0 CD B:GLU156 3.9 45.2 1.0 ND1 B:HIS154 3.9 44.6 1.0 CD2 B:HIS154 4.0 45.1 1.0 CD2 B:HIS303 4.2 45.4 1.0 OE2 B:GLU156 4.5 48.1 1.0 ND1 B:HIS303 4.5 44.9 1.0 NH2 B:ARG321 4.5 52.4 1.0 CG B:HIS154 4.5 44.8 1.0 CB B:GLU156 4.9 40.5 1.0 CG B:HIS303 4.9 44.1 1.0 CA B:GLU156 5.0 39.1 1.0 CG B:GLU156 5.0 42.6 1.0

Iron binding site 2 out of 3 in the Crystal Structure of Non-Heme Iron Oxygenase Orfp in Complex with Fe and D-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 D-Arg within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe401 b:70.2 occ:1.00 OE1 C:GLU156 2.3 37.1 1.0 NE2 C:HIS154 2.5 32.2 1.0 NE2 C:HIS303 2.5 26.3 1.0 O C:HOH538 2.8 39.8 1.0 CE1 C:HIS154 3.0 31.4 1.0 CE1 C:HIS303 3.2 26.5 1.0 CD C:GLU156 3.3 35.6 1.0 CA C:DAR402 3.5 51.4 1.0 CD2 C:HIS303 3.5 26.1 1.0 OE2 C:GLU156 3.6 36.3 1.0 CD2 C:HIS154 3.6 31.1 1.0 O C:DAR402 4.0 54.0 1.0 CG C:DAR402 4.1 45.6 1.0 N C:DAR402 4.1 52.4 1.0 C C:DAR402 4.3 53.2 1.0 ND1 C:HIS154 4.3 31.4 1.0 ND1 C:HIS303 4.3 25.9 1.0 NH2 C:ARG321 4.4 39.5 1.0 CB C:DAR402 4.4 49.7 1.0 CG C:HIS303 4.5 26.3 1.0 CG C:HIS154 4.6 31.3 1.0 CG C:GLU156 4.7 33.6 1.0 NE C:ARG321 4.8 38.5 1.0 CD2 C:LEU151 4.9 38.0 1.0 CZ C:ARG321 5.0 39.5 1.0 CB C:GLU156 5.0 31.9 1.0

Iron binding site 3 out of 3 in the Crystal Structure of Non-Heme Iron Oxygenase Orfp in Complex with Fe and D-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 D-Arg within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe401 b:67.9 occ:1.00 OE1 D:GLU156 2.0 37.0 1.0 NE2 D:HIS154 2.5 35.1 1.0 NE2 D:HIS303 2.5 32.1 1.0 CD D:GLU156 3.0 35.7 1.0 CE1 D:HIS154 3.0 34.8 1.0 CE1 D:HIS303 3.1 32.2 1.0 OE2 D:GLU156 3.2 36.9 1.0 CD2 D:HIS303 3.6 32.3 1.0 CD2 D:HIS154 3.7 34.1 1.0 N D:DAR402 3.7 50.1 1.0 CA D:DAR402 3.9 49.7 1.0 CG D:DAR402 4.0 45.8 1.0 ND1 D:HIS154 4.3 34.2 1.0 ND1 D:HIS303 4.3 32.1 1.0 CG D:GLU156 4.4 35.8 1.0 CB D:DAR402 4.6 48.4 1.0 CG D:HIS303 4.6 32.8 1.0 CG D:HIS154 4.7 33.8 1.0 CD2 D:LEU151 4.8 39.9 1.0 CB D:GLU156 4.8 34.1 1.0 O D:HOH506 4.8 37.6 1.0 NE D:ARG321 5.0 42.2 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