Iron in PDB 6o6l: The Structure of Egtb(Cabther) in Complex with Hercynine

The structure of The Structure of Egtb(Cabther) in Complex with Hercynine, PDB code: 6o6l was solved by S.Irani, Y.Zhang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.83 / 2.25
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	85.164, 137.513, 85.218, 90.00, 92.37, 90.00
R / Rfree (%)	18.7 / 22.1

The binding sites of Iron atom in the The Structure of Egtb(Cabther) in Complex with Hercynine (pdb code 6o6l). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the The Structure of Egtb(Cabther) in Complex with Hercynine, PDB code: 6o6l:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the The Structure of Egtb(Cabther) in Complex with Hercynine


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of The Structure of Egtb(Cabther) in Complex with Hercynine within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe502 b:17.6 occ:1.00 O A:HOH690 1.8 20.2 1.0 NE2 A:HIS153 2.2 20.8 1.0 NE2 A:HIS157 2.2 20.3 1.0 NAT A:AVJ501 2.3 15.9 1.0 NE2 A:HIS62 2.3 16.5 1.0 O A:HOH743 2.3 19.7 1.0 CE1 A:HIS153 2.9 17.4 1.0 CE1 A:HIS157 3.0 15.9 1.0 CAZ A:AVJ501 3.3 16.8 1.0 CE1 A:HIS62 3.3 17.0 1.0 CD2 A:HIS62 3.3 16.0 1.0 CD2 A:HIS153 3.3 17.8 1.0 CD2 A:HIS157 3.3 15.1 1.0 CAM A:AVJ501 3.3 15.5 1.0 O A:HOH672 3.7 18.3 1.0 ND1 A:HIS153 4.1 16.4 1.0 OG A:SER92 4.2 23.4 1.0 ND1 A:HIS157 4.2 14.2 1.0 CG A:HIS153 4.3 18.5 1.0 CB A:SER92 4.3 19.0 1.0 CG A:HIS157 4.3 14.3 1.0 ND1 A:HIS62 4.4 16.8 1.0 CG A:HIS62 4.4 15.8 1.0 CAY A:AVJ501 4.5 15.2 1.0 NAR A:AVJ501 4.5 16.0 1.0

Iron binding site 2 out of 4 in the The Structure of Egtb(Cabther) in Complex with Hercynine


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of The Structure of Egtb(Cabther) in Complex with Hercynine within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe502 b:12.6 occ:1.00 O B:HOH609 2.1 15.5 1.0 NE2 B:HIS153 2.1 13.7 1.0 NAT B:AVJ501 2.1 14.5 1.0 NE2 B:HIS157 2.1 15.4 1.0 NE2 B:HIS62 2.2 14.9 1.0 O B:HOH742 2.7 18.1 1.0 CE1 B:HIS153 2.9 13.2 1.0 CAZ B:AVJ501 3.0 13.8 1.0 CE1 B:HIS157 3.1 13.0 1.0 CD2 B:HIS62 3.1 13.2 1.0 CD2 B:HIS157 3.2 12.6 1.0 CE1 B:HIS62 3.2 13.4 1.0 CD2 B:HIS153 3.2 12.8 1.0 CAM B:AVJ501 3.3 13.0 1.0 O B:HOH607 3.8 21.2 1.0 OG B:SER92 4.0 17.0 1.0 ND1 B:HIS153 4.1 13.6 1.0 ND1 B:HIS157 4.2 13.3 1.0 CG B:HIS153 4.3 13.7 1.0 CB B:SER92 4.3 17.4 1.0 ND1 B:HIS62 4.3 14.0 1.0 CG B:HIS62 4.3 13.9 1.0 CG B:HIS157 4.3 13.1 1.0 NAR B:AVJ501 4.3 13.2 1.0 CAY B:AVJ501 4.4 13.0 1.0

Iron binding site 3 out of 4 in the The Structure of Egtb(Cabther) in Complex with Hercynine


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of The Structure of Egtb(Cabther) in Complex with Hercynine within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe502 b:17.6 occ:1.00 NE2 C:HIS157 2.1 15.7 1.0 O C:HOH654 2.1 15.2 1.0 NAT C:AVJ501 2.2 15.2 1.0 NE2 C:HIS153 2.2 13.8 1.0 NE2 C:HIS62 2.3 14.5 1.0 CE1 C:HIS157 3.0 14.0 1.0 CE1 C:HIS153 3.1 13.1 1.0 O C:HOH753 3.2 23.6 1.0 CD2 C:HIS62 3.2 13.1 1.0 CAZ C:AVJ501 3.2 15.2 1.0 CD2 C:HIS157 3.2 13.0 1.0 CAM C:AVJ501 3.2 14.2 1.0 CD2 C:HIS153 3.3 13.2 1.0 CE1 C:HIS62 3.4 14.2 1.0 O C:HOH623 4.0 18.0 1.0 OG C:SER92 4.1 16.9 1.0 ND1 C:HIS157 4.1 12.4 1.0 CB C:SER92 4.2 16.5 1.0 ND1 C:HIS153 4.2 14.3 1.0 CG C:HIS157 4.3 12.8 1.0 CG C:HIS62 4.4 13.7 1.0 CG C:HIS153 4.4 13.5 1.0 CAY C:AVJ501 4.4 15.7 1.0 NAR C:AVJ501 4.4 15.2 1.0 ND1 C:HIS62 4.4 13.9 1.0

Iron binding site 4 out of 4 in the The Structure of Egtb(Cabther) in Complex with Hercynine


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of The Structure of Egtb(Cabther) in Complex with Hercynine within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe502 b:17.6 occ:1.00 O D:HOH643 1.8 22.9 1.0 NAT D:AVJ501 2.1 16.5 1.0 NE2 D:HIS157 2.2 15.8 1.0 NE2 D:HIS153 2.3 20.4 1.0 NE2 D:HIS62 2.3 16.9 1.0 O D:HOH732 2.5 18.8 1.0 CE1 D:HIS157 3.0 15.0 1.0 CAZ D:AVJ501 3.1 17.3 1.0 CD2 D:HIS62 3.1 15.8 1.0 CE1 D:HIS153 3.2 17.5 1.0 CAM D:AVJ501 3.2 16.0 1.0 CD2 D:HIS157 3.3 15.1 1.0 CD2 D:HIS153 3.3 17.0 1.0 CE1 D:HIS62 3.3 17.2 1.0 OG D:SER92 4.0 23.1 1.0 ND1 D:HIS157 4.2 14.5 1.0 CB D:SER92 4.3 20.5 1.0 ND1 D:HIS153 4.3 22.6 1.0 CG D:HIS62 4.3 15.7 1.0 NAR D:AVJ501 4.3 16.7 1.0 CG D:HIS157 4.3 14.0 1.0 CAY D:AVJ501 4.3 15.8 1.0 ND1 D:HIS62 4.4 16.3 1.0 CG D:HIS153 4.4 17.3 1.0

N.Naowarojna, S.Irani, R.Cheng, W.Hu, L.Zhang, X.Li, J.Chen, Y.Zhang, P.Liu. Crystal Structure of the Ergothioneine Sulfoxide Synthase From Candidatus Chloracidobacterium Thermophilum and Structure-Guided Engineering to Modulate Its Substrate Selectivity Acs Catalysis 2019.
ISSN: ESSN 2155-5435
DOI: 10.1021/ACSCATAL.9B02054