Iron in PDB 4ne0: Crystal Structure of Non-Heme Iron Oxygenase Orfp D157A Mutant in Complex with (3S)-Hydroxy-L-Arg

The structure of Crystal Structure of Non-Heme Iron Oxygenase Orfp D157A Mutant in Complex with (3S)-Hydroxy-L-Arg, PDB code: 4ne0 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 / 2.17
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	67.861, 117.330, 95.815, 90.00, 91.33, 90.00
R / Rfree (%)	21 / 26.9

The binding sites of Iron atom in the Crystal Structure of Non-Heme Iron Oxygenase Orfp D157A Mutant in Complex with (3S)-Hydroxy-L-Arg (pdb code 4ne0). 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 D157A Mutant in Complex with (3S)-Hydroxy-L-Arg, PDB code: 4ne0:
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 D157A Mutant in Complex with (3S)-Hydroxy-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 D157A Mutant in Complex with (3S)-Hydroxy-L-Arg within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe401 b:73.5 occ:1.00 OE1 A:GLU156 2.3 47.5 1.0 NE2 A:HIS303 2.6 38.7 1.0 NE2 A:HIS154 2.8 48.7 1.0 CE1 A:HIS154 2.9 50.3 1.0 CD A:GLU156 3.2 51.3 1.0 CE1 A:HIS303 3.4 38.4 1.0 OE2 A:GLU156 3.4 53.3 1.0 CD2 A:HIS303 3.5 33.2 1.0 CD2 A:HIS154 4.0 50.1 1.0 ND1 A:HIS154 4.1 51.9 1.0 O A:HOH637 4.2 59.3 1.0 NH2 A:ARG321 4.2 45.0 1.0 ND1 A:HIS303 4.5 34.9 1.0 CG A:HIS303 4.6 33.1 1.0 CG A:GLU156 4.6 43.1 1.0 CG A:HIS154 4.7 44.5 1.0 O A:HOH611 4.8 40.7 1.0 CB A:GLU156 4.9 32.6 1.0 CD2 A:LEU151 5.0 53.3 1.0

Iron binding site 2 out of 4 in the Crystal Structure of Non-Heme Iron Oxygenase Orfp D157A Mutant in Complex with (3S)-Hydroxy-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 D157A Mutant in Complex with (3S)-Hydroxy-L-Arg within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe401 b:90.8 occ:1.00 NE2 B:HIS154 2.5 56.6 1.0 NE2 B:HIS303 2.5 37.0 1.0 OE1 B:GLU156 2.6 48.6 1.0 CE1 B:HIS154 3.3 46.4 1.0 CD2 B:HIS303 3.4 36.1 1.0 CE1 B:HIS303 3.4 36.4 1.0 NH2 B:ARG321 3.5 56.1 1.0 CD2 B:HIS154 3.6 52.4 1.0 CD B:GLU156 3.7 49.8 1.0 OE2 B:GLU156 4.0 56.8 1.0 ND1 B:HIS303 4.4 37.1 1.0 CG B:HIS303 4.5 36.2 1.0 ND1 B:HIS154 4.5 52.1 1.0 CZ B:ARG321 4.7 53.6 1.0 CG B:HIS154 4.7 47.1 1.0 CG B:GLU156 5.0 42.0 1.0

Iron binding site 3 out of 4 in the Crystal Structure of Non-Heme Iron Oxygenase Orfp D157A Mutant in Complex with (3S)-Hydroxy-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 D157A Mutant in Complex with (3S)-Hydroxy-L-Arg within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe401 b:68.4 occ:1.00 NE2 C:HIS303 2.2 25.0 1.0 OB C:ZZU403 2.3 44.5 1.0 O3 C:SIN402 2.6 55.5 1.0 OE1 C:GLU156 2.7 41.4 1.0 NE2 C:HIS154 2.7 37.3 1.0 O4 C:SIN402 3.1 43.1 1.0 C4 C:SIN402 3.1 51.1 1.0 CD2 C:HIS303 3.1 25.8 1.0 CE1 C:HIS303 3.2 26.6 1.0 CE1 C:HIS154 3.3 29.1 1.0 CB C:ZZU403 3.5 54.7 1.0 NH1 C:ARG321 3.6 46.0 1.0 CD C:GLU156 3.8 43.0 1.0 CD2 C:HIS154 3.9 32.9 1.0 CA C:ZZU403 4.0 64.9 1.0 CG C:ZZU403 4.2 48.5 1.0 OXT C:ZZU403 4.2 61.5 1.0 OE2 C:GLU156 4.2 53.4 1.0 ND1 C:HIS303 4.3 29.6 1.0 CG C:HIS303 4.3 27.6 1.0 C C:ZZU403 4.3 66.5 1.0 CD2 C:LEU151 4.4 43.5 1.0 C3 C:SIN402 4.4 43.2 1.0 ND1 C:HIS154 4.5 33.4 1.0 CZ C:ARG321 4.7 40.1 1.0 CG C:HIS154 4.9 29.8 1.0 CD2 C:LEU167 5.0 41.4 1.0

Iron binding site 4 out of 4 in the Crystal Structure of Non-Heme Iron Oxygenase Orfp D157A Mutant in Complex with (3S)-Hydroxy-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 D157A Mutant in Complex with (3S)-Hydroxy-L-Arg within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe401 b:76.1 occ:1.00 NE2 D:HIS303 2.0 30.0 1.0 O3 D:SIN402 2.5 56.5 1.0 O4 D:SIN402 2.6 66.2 1.0 OE1 D:GLU156 2.6 38.2 1.0 NE2 D:HIS154 2.7 36.8 1.0 C4 D:SIN402 2.8 66.0 1.0 OB D:ZZU403 2.9 58.3 1.0 CD2 D:HIS303 3.0 30.3 1.0 CE1 D:HIS303 3.0 33.6 1.0 CE1 D:HIS154 3.2 35.9 1.0 NH2 D:ARG321 3.2 53.1 1.0 CD2 D:HIS154 3.9 30.7 1.0 CD D:GLU156 3.9 47.8 1.0 ND1 D:HIS303 4.1 33.7 1.0 CG D:HIS303 4.1 31.3 1.0 CB D:ZZU403 4.3 55.3 1.0 C3 D:SIN402 4.3 54.8 1.0 ND1 D:HIS154 4.4 31.1 1.0 OE2 D:GLU156 4.4 52.8 1.0 CZ D:ARG321 4.5 45.6 1.0 CD2 D:LEU151 4.5 38.0 1.0 O D:ZZU403 4.5 59.2 1.0 O D:HIS303 4.7 33.3 1.0 CG D:HIS154 4.8 29.8 1.0 CG D:ZZU403 4.8 48.1 1.0 CA D:ZZU403 4.8 66.4 1.0 C D:ZZU403 4.8 63.9 1.0 CD2 D:LEU167 4.9 48.3 1.0 C2 D:SIN402 4.9 57.9 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