Iron in PDB 8qfl: Ergothioneine Dioxygenase From Thermocatellispora Tengchongensis in Complex with Iron

The structure of Ergothioneine Dioxygenase From Thermocatellispora Tengchongensis in Complex with Iron, PDB code: 8qfl was solved by C.M.Vasseur, F.P.Seebeck, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	44.37 / 1.75
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	44.611, 58.946, 134.776, 90, 90, 90
R / Rfree (%)	17.3 / 21.2

The structure of Ergothioneine Dioxygenase From Thermocatellispora Tengchongensis in Complex with Iron also contains other interesting chemical elements:

Magnesium

(Mg)

1 atom

The binding sites of Iron atom in the Ergothioneine Dioxygenase From Thermocatellispora Tengchongensis in Complex with Iron (pdb code 8qfl). 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 Dioxygenase From Thermocatellispora Tengchongensis in Complex with Iron, PDB code: 8qfl:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Ergothioneine Dioxygenase From Thermocatellispora Tengchongensis in Complex with Iron


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Ergothioneine Dioxygenase From Thermocatellispora Tengchongensis in Complex with Iron within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe201 b:26.6 occ:1.00 NE2 A:HIS134 2.0 25.2 1.0 NE2 A:HIS88 2.0 26.6 1.0 O A:HOH336 2.1 31.2 1.0 NE2 A:HIS90 2.1 26.1 1.0 O A:ACT202 2.2 30.1 0.8 O A:HOH331 2.3 29.1 1.0 CE1 A:HIS90 2.9 24.9 1.0 CE1 A:HIS134 2.9 26.0 1.0 CE1 A:HIS88 3.0 28.9 1.0 CD2 A:HIS88 3.0 28.1 1.0 HE1 A:HIS90 3.0 29.9 1.0 CD2 A:HIS134 3.1 29.2 1.0 HE1 A:HIS134 3.1 31.2 1.0 C A:ACT202 3.2 25.9 0.8 CD2 A:HIS90 3.2 26.4 1.0 HD2 A:HIS88 3.2 33.8 1.0 HE1 A:HIS88 3.2 34.8 1.0 HD2 A:HIS134 3.3 35.1 1.0 O A:HOH367 3.3 49.2 1.0 HD2 A:HIS90 3.4 31.7 1.0 OXT A:ACT202 3.5 26.8 0.8 HE2 A:TYR149 3.9 33.6 1.0 OH A:TYR149 4.1 31.4 1.0 HZ A:PHE128 4.1 37.5 1.0 ND1 A:HIS134 4.1 29.1 1.0 ND1 A:HIS90 4.1 26.8 1.0 ND1 A:HIS88 4.1 30.2 1.0 CG A:HIS134 4.2 24.6 1.0 CG A:HIS88 4.2 24.7 1.0 CG A:HIS90 4.2 24.8 1.0 HD22 A:LEU136 4.4 35.2 1.0 CH3 A:ACT202 4.5 27.7 0.8 H1 A:ACT202 4.6 33.2 0.8 CE2 A:TYR149 4.7 28.0 1.0 HH A:TYR149 4.7 37.6 1.0 CZ A:PHE128 4.7 31.2 1.0 HD13 A:LEU136 4.8 50.1 1.0 HG21 A:THR85 4.9 36.8 1.0 HD1 A:HIS134 4.9 35.0 1.0 HD1 A:HIS90 4.9 32.1 1.0 CZ A:TYR149 4.9 32.6 1.0 HD1 A:HIS88 4.9 36.3 1.0 HD11 A:LEU156 5.0 58.8 1.0

Iron binding site 2 out of 2 in the Ergothioneine Dioxygenase From Thermocatellispora Tengchongensis in Complex with Iron


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Ergothioneine Dioxygenase From Thermocatellispora Tengchongensis in Complex with Iron within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe201 b:25.1 occ:1.00 NE2 B:HIS90 2.0 24.8 1.0 NE2 B:HIS134 2.0 25.9 1.0 NE2 B:HIS88 2.1 25.7 1.0 O B:HOH347 2.1 34.1 1.0 O B:HOH336 2.2 29.1 1.0 OXT B:ACT202 2.2 30.5 1.0 CE1 B:HIS134 3.0 30.8 1.0 CE1 B:HIS90 3.0 30.3 1.0 CD2 B:HIS88 3.0 27.3 1.0 CE1 B:HIS88 3.1 29.6 1.0 CD2 B:HIS90 3.1 26.2 1.0 HE1 B:HIS134 3.1 36.9 1.0 HE1 B:HIS90 3.1 36.3 1.0 CD2 B:HIS134 3.1 25.4 1.0 C B:ACT202 3.2 34.8 1.0 HD2 B:HIS88 3.2 32.7 1.0 HE1 B:HIS88 3.3 35.6 1.0 HD2 B:HIS90 3.3 31.5 1.0 HD2 B:HIS134 3.4 30.4 1.0 O B:HOH374 3.4 45.3 1.0 O B:ACT202 3.5 32.0 1.0 HE1 B:TYR149 3.8 33.3 1.0 HZ B:PHE128 3.9 35.3 1.0 OH B:TYR149 4.1 33.1 1.0 ND1 B:HIS90 4.1 28.5 1.0 ND1 B:HIS134 4.1 27.4 1.0 ND1 B:HIS88 4.2 28.0 1.0 CG B:HIS90 4.2 28.0 1.0 CG B:HIS88 4.2 26.1 1.0 CG B:HIS134 4.3 23.4 1.0 CH3 B:ACT202 4.5 33.8 1.0 H3 B:ACT202 4.5 40.6 1.0 CE1 B:TYR149 4.6 27.7 1.0 CZ B:PHE128 4.6 29.4 1.0 HH B:TYR149 4.7 39.7 1.0 HD12 B:LEU136 4.7 38.6 1.0 HD12 B:LEU156 4.8 61.5 1.0 HG21 B:THR85 4.8 38.2 1.0 HG B:LEU136 4.9 41.4 1.0 CZ B:TYR149 4.9 34.6 1.0 HD1 B:HIS90 4.9 34.2 1.0 HD1 B:HIS134 4.9 32.9 1.0 HD1 B:HIS88 5.0 33.6 1.0

E.Nalivaiko, C.M.Vasseur, F.P.Seebeck. Enzyme-Catalyzed Oxidative Degradation of Ergothioneine. Angew.Chem.Int.Ed.Engl. 18445 2023.
ISSN: ESSN 1521-3773
PubMed: 38095354
DOI: 10.1002/ANIE.202318445