Iron in PDB 6gem: Feii-Dependent Halogenase Wi-WELO15

The structure of Feii-Dependent Halogenase Wi-WELO15, PDB code: 6gem was solved by V.Srinivasan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	49.19 / 3.46
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	195.830, 155.451, 133.234, 90.00, 126.91, 90.00
R / Rfree (%)	19.1 / 24.2

The binding sites of Iron atom in the Feii-Dependent Halogenase Wi-WELO15 (pdb code 6gem). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Feii-Dependent Halogenase Wi-WELO15, PDB code: 6gem:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the Feii-Dependent Halogenase Wi-WELO15


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Feii-Dependent Halogenase Wi-WELO15 within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe301 b:44.7 occ:1.00 O2 A:AKG302 2.2 30.1 1.0 O5 A:AKG302 2.5 30.8 1.0 NE2 A:HIS164 2.7 14.6 1.0 C1 A:AKG302 2.7 40.1 1.0 NE2 A:HIS259 2.8 11.7 1.0 C2 A:AKG302 3.0 42.1 1.0 CD2 A:HIS164 3.3 11.7 1.0 O1 A:AKG302 3.7 33.7 1.0 CD2 A:HIS259 3.8 8.9 1.0 CE1 A:HIS259 3.8 9.1 1.0 CE1 A:HIS164 3.8 13.6 1.0 OG A:SER189 4.0 9.0 1.0 C3 A:AKG302 4.4 30.0 1.0 CE1 A:PHE276 4.5 11.5 1.0 CG A:HIS164 4.6 11.2 1.0 ND1 A:HIS164 4.8 11.7 1.0 C4 A:AKG302 4.9 37.1 1.0 ND1 A:HIS259 4.9 5.8 1.0 CG A:HIS259 4.9 6.4 1.0 CB A:SER189 5.0 4.8 1.0

Iron binding site 2 out of 4 in the Feii-Dependent Halogenase Wi-WELO15


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Feii-Dependent Halogenase Wi-WELO15 within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe301 b:52.6 occ:1.00 O2 B:AKG302 2.1 33.7 1.0 C1 B:AKG302 2.3 48.2 1.0 O5 B:AKG302 2.4 37.7 1.0 C2 B:AKG302 2.7 49.2 1.0 NE2 B:HIS164 2.8 28.6 1.0 NE2 B:HIS259 2.8 22.6 1.0 O1 B:AKG302 3.2 46.0 1.0 CD2 B:HIS164 3.5 20.8 1.0 CE1 B:HIS259 3.7 18.3 1.0 OG B:SER189 3.8 33.4 1.0 CD2 B:HIS259 3.9 15.8 1.0 CE1 B:PHE276 3.9 24.6 1.0 CE1 B:HIS164 3.9 24.1 1.0 C3 B:AKG302 4.2 42.0 1.0 CZ B:PHE276 4.5 29.2 1.0 CB B:SER189 4.7 19.4 1.0 C4 B:AKG302 4.7 47.2 1.0 CG B:HIS164 4.7 17.9 1.0 ND1 B:HIS259 4.9 12.8 1.0 CD1 B:PHE276 4.9 25.1 1.0 ND1 B:HIS164 4.9 20.0 1.0

Iron binding site 3 out of 4 in the Feii-Dependent Halogenase Wi-WELO15


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Feii-Dependent Halogenase Wi-WELO15 within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe301 b:49.8 occ:1.00 O1 C:AKG302 1.9 40.8 1.0 NE2 C:HIS164 2.3 37.5 1.0 O5 C:AKG302 2.5 45.4 1.0 NE2 C:HIS259 2.6 55.9 1.0 C1 C:AKG302 2.6 53.0 1.0 C2 C:AKG302 2.9 55.1 1.0 CD2 C:HIS164 3.0 39.9 1.0 CE1 C:HIS164 3.5 41.8 1.0 CD2 C:HIS259 3.5 47.6 1.0 CE1 C:HIS259 3.6 43.7 1.0 O2 C:AKG302 3.8 54.1 1.0 OG C:SER189 3.9 20.8 1.0 CG C:HIS164 4.3 38.1 1.0 C3 C:AKG302 4.4 48.6 1.0 ND1 C:HIS164 4.4 44.2 1.0 CE1 C:PHE276 4.6 36.4 1.0 CG C:HIS259 4.7 38.9 1.0 ND1 C:HIS259 4.7 43.1 1.0 CB C:SER189 4.8 21.6 1.0

Iron binding site 4 out of 4 in the Feii-Dependent Halogenase Wi-WELO15


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Feii-Dependent Halogenase Wi-WELO15 within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe301 b:41.0 occ:1.00 O1 D:AKG302 2.1 33.5 1.0 C1 D:AKG302 2.6 45.4 1.0 O5 D:AKG302 2.6 34.7 1.0 NE2 D:HIS164 2.6 19.6 1.0 NE2 D:HIS259 2.6 22.6 1.0 C2 D:AKG302 3.0 46.5 1.0 CD2 D:HIS164 3.2 15.9 1.0 O2 D:AKG302 3.5 38.4 1.0 CD2 D:HIS259 3.5 17.1 1.0 CE1 D:HIS259 3.6 18.0 1.0 CE1 D:HIS164 3.8 17.0 1.0 OG D:SER189 3.9 14.7 1.0 C3 D:AKG302 4.5 35.6 1.0 CG D:HIS164 4.5 12.7 1.0 CB D:SER189 4.6 9.8 1.0 ND1 D:HIS259 4.7 13.4 1.0 CG D:HIS259 4.7 10.8 1.0 ND1 D:HIS164 4.7 15.3 1.0 CE1 D:PHE276 4.7 14.1 1.0

V.Srinivasan, L.Schmermund, T.Faber, K.Harms, V.Srinivasan, E.Meggers, S.Hoebenreich. Directed Evolution of An Feii-Dependent Halogenase For Asymmetric C(SP3)-H Chlorination Chemrxiv 2019.
DOI: 10.26434/CHEMRXIV.10087298.V1