Iron in PDB 4x8e: Ergothioneine-Biosynthetic Sulfoxide Synthase Egtb in Complex with N, N,N-Trimethyl-Histidine

The structure of Ergothioneine-Biosynthetic Sulfoxide Synthase Egtb in Complex with N, N,N-Trimethyl-Histidine, PDB code: 4x8e was solved by A.Vit, K.V.Goncharenko, W.Blankenfeldt, F.P.Seebeck, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.97 / 1.60
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	135.241, 135.241, 142.043, 90.00, 90.00, 90.00
R / Rfree (%)	14.5 / 16.3

The structure of Ergothioneine-Biosynthetic Sulfoxide Synthase Egtb in Complex with N, N,N-Trimethyl-Histidine also contains other interesting chemical elements:

Magnesium	(Mg)	2 atoms
Calcium	(Ca)	2 atoms
Chlorine	(Cl)	7 atoms

The binding sites of Iron atom in the Ergothioneine-Biosynthetic Sulfoxide Synthase Egtb in Complex with N, N,N-Trimethyl-Histidine (pdb code 4x8e). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Ergothioneine-Biosynthetic Sulfoxide Synthase Egtb in Complex with N, N,N-Trimethyl-Histidine, PDB code: 4x8e:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Ergothioneine-Biosynthetic Sulfoxide Synthase Egtb in Complex with N, N,N-Trimethyl-Histidine


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Ergothioneine-Biosynthetic Sulfoxide Synthase Egtb in Complex with N, N,N-Trimethyl-Histidine within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe515 b:15.0 occ:1.00 NE2 A:HIS134 2.1 16.3 1.0 O A:HOH702 2.1 18.5 1.0 NAT A:AVJ501 2.1 15.4 1.0 NE2 A:HIS138 2.1 16.2 1.0 NE2 A:HIS51 2.1 14.8 1.0 O A:HOH712 2.2 17.6 1.0 CD2 A:HIS134 3.0 17.3 1.0 CE1 A:HIS134 3.0 17.2 1.0 CAZ A:AVJ501 3.1 16.6 1.0 CE1 A:HIS138 3.1 16.1 1.0 CE1 A:HIS51 3.1 18.9 1.0 CD2 A:HIS138 3.1 17.2 1.0 CAM A:AVJ501 3.1 19.7 1.0 CD2 A:HIS51 3.2 15.4 1.0 HD2 A:HIS134 3.2 20.7 1.0 HE1 A:HIS51 3.2 22.7 1.0 HAZ A:AVJ501 3.2 20.0 1.0 HE1 A:HIS138 3.2 19.3 1.0 HE1 A:HIS134 3.2 20.7 1.0 HD2 A:HIS138 3.3 20.6 1.0 HD2 A:HIS51 3.3 18.5 1.0 HAM A:AVJ501 3.4 23.7 1.0 HG3 A:GLN55 3.6 23.7 1.0 O A:HOH837 4.0 32.0 1.0 ND1 A:HIS134 4.1 17.9 1.0 CG A:HIS134 4.2 17.4 1.0 ND1 A:HIS138 4.2 17.3 1.0 ND1 A:HIS51 4.2 18.1 1.0 CG A:HIS138 4.2 16.8 1.0 NAR A:AVJ501 4.2 17.4 1.0 CG A:HIS51 4.3 17.5 1.0 CAY A:AVJ501 4.3 16.9 1.0 O A:HOH883 4.4 30.0 1.0 HE2 A:TYR377 4.5 24.9 1.0 OE1 A:GLN55 4.5 23.0 1.0 CG A:GLN55 4.5 19.7 1.0 HO3 A:GOL506 4.6 41.3 1.0 OH A:TYR377 4.6 22.1 1.0 H31 A:GOL506 4.6 55.0 1.0 CD A:GLN55 4.8 19.1 1.0 HD1 A:HIS134 4.9 21.4 1.0 HD1 A:HIS138 5.0 20.7 1.0 HD1 A:HIS51 5.0 21.8 1.0

Iron binding site 2 out of 2 in the Ergothioneine-Biosynthetic Sulfoxide Synthase Egtb in Complex with N, N,N-Trimethyl-Histidine


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Ergothioneine-Biosynthetic Sulfoxide Synthase Egtb in Complex with N, N,N-Trimethyl-Histidine within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe508 b:25.0 occ:1.00 NE2 B:HIS138 2.1 29.7 1.0 NAT B:AVJ501 2.1 27.9 1.0 NE2 B:HIS51 2.1 30.4 1.0 O B:HOH644 2.1 28.7 1.0 NE2 B:HIS134 2.1 30.6 1.0 O B:HOH640 2.2 28.2 1.0 CE1 B:HIS51 3.0 30.8 1.0 CAZ B:AVJ501 3.1 27.4 1.0 CE1 B:HIS138 3.1 28.3 1.0 CD2 B:HIS134 3.1 29.8 1.0 CD2 B:HIS138 3.1 28.2 1.0 CE1 B:HIS134 3.1 31.0 1.0 CD2 B:HIS51 3.2 30.6 1.0 HE1 B:HIS51 3.2 36.9 1.0 HAZ B:AVJ501 3.2 32.9 1.0 CAM B:AVJ501 3.2 27.4 1.0 HD2 B:HIS134 3.2 35.8 1.0 HE1 B:HIS138 3.2 33.9 1.0 HD2 B:HIS138 3.3 33.9 1.0 HE1 B:HIS134 3.3 37.2 1.0 HD2 B:HIS51 3.4 36.7 1.0 HAM B:AVJ501 3.5 32.9 1.0 HG3 B:GLN55 3.6 39.9 1.0 O B:HOH851 4.1 42.4 1.0 ND1 B:HIS51 4.2 31.1 1.0 ND1 B:HIS138 4.2 27.6 1.0 O B:HOH985 4.2 52.4 1.0 ND1 B:HIS134 4.2 30.6 1.0 CG B:HIS134 4.2 29.9 1.0 CG B:HIS138 4.2 27.4 1.0 NAR B:AVJ501 4.3 28.0 1.0 CG B:HIS51 4.3 31.0 1.0 CAY B:AVJ501 4.3 28.1 1.0 HE2 B:TYR377 4.5 42.4 1.0 OE1 B:GLN55 4.5 33.8 1.0 CG B:GLN55 4.5 33.3 1.0 OH B:TYR377 4.6 35.5 1.0 CD B:GLN55 4.8 35.7 1.0 HD1 B:HIS51 4.9 37.4 1.0 HD1 B:HIS138 5.0 33.2 1.0 HG2 B:GLN55 5.0 39.9 1.0 HD1 B:HIS134 5.0 36.8 1.0

K.V.Goncharenko, A.Vit, W.Blankenfeldt, F.P.Seebeck. Structure of the Sulfoxide Synthase Egtb From the Ergothioneine Biosynthetic Pathway. Angew.Chem.Int.Ed.Engl. 2015.
ISSN: ESSN 1521-3773
PubMed: 25597398
DOI: 10.1002/ANIE.201410045