Iron in PDB 6a4z: Oxidase Chap

The structure of Oxidase Chap, PDB code: 6a4z was solved by B.Zhang, H.M.Ge, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.80 / 1.70
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	53.830, 47.120, 53.920, 90.00, 109.60, 90.00
R / Rfree (%)	17.9 / 20.7

The binding sites of Iron atom in the Oxidase Chap (pdb code 6a4z). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Oxidase Chap, PDB code: 6a4z:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Oxidase Chap


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Oxidase Chap within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe201 b:27.1 occ:1.00 O A:HOH307 2.2 15.1 1.0 OE1 A:GLU119 2.2 12.3 1.0 NE2 A:HIS63 2.2 15.6 1.0 OH A:TYR125 2.2 16.4 1.0 NE2 B:HIS7 2.3 13.6 1.0 O B:HOH379 2.3 15.9 1.0 CE1 A:HIS63 3.1 14.3 1.0 CE1 B:HIS7 3.2 14.8 1.0 CD A:GLU119 3.2 15.0 1.0 CD2 B:HIS7 3.3 17.3 1.0 CD2 A:HIS63 3.3 14.2 1.0 CZ A:TYR125 3.3 19.8 1.0 OE2 A:GLU119 3.6 16.2 1.0 CE2 A:TYR125 3.7 24.3 1.0 OH A:TYR109 4.1 14.3 1.0 CB A:ALA65 4.1 12.8 1.0 ND1 A:HIS63 4.2 15.7 1.0 O B:HOH328 4.2 22.2 1.0 O A:HOH406 4.3 52.0 1.0 ND1 B:HIS7 4.3 13.8 1.0 CG A:HIS63 4.4 16.6 1.0 CG B:HIS7 4.4 14.8 1.0 CE2 A:TYR109 4.4 12.4 1.0 CG A:GLU119 4.5 13.5 1.0 CE1 A:TYR125 4.5 17.9 1.0 CB A:GLU119 4.7 13.3 1.0 CZ A:TYR109 4.7 15.2 1.0

Iron binding site 2 out of 2 in the Oxidase Chap


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Oxidase Chap within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe202 b:32.8 occ:1.00 O A:HOH387 2.2 23.2 1.0 NE2 A:HIS7 2.2 18.8 1.0 OE1 B:GLU119 2.2 19.4 1.0 O B:HOH327 2.2 22.3 1.0 OH B:TYR125 2.3 22.3 1.0 NE2 B:HIS63 2.3 21.8 1.0 CE1 A:HIS7 3.1 21.8 1.0 CE1 B:HIS63 3.2 20.4 1.0 CD2 A:HIS7 3.2 20.7 1.0 CD B:GLU119 3.3 24.5 1.0 CD2 B:HIS63 3.4 18.1 1.0 CZ B:TYR125 3.4 34.6 1.0 OE2 B:GLU119 3.6 23.5 1.0 CE2 B:TYR125 3.8 37.0 1.0 O B:HOH369 4.1 37.7 1.0 OH B:TYR109 4.2 21.3 1.0 CB B:ALA65 4.2 18.1 1.0 O B:HOH313 4.2 53.0 1.0 ND1 A:HIS7 4.2 19.2 1.0 O A:HOH310 4.3 25.4 1.0 CG A:HIS7 4.3 23.1 1.0 ND1 B:HIS63 4.3 20.9 1.0 CG B:HIS63 4.4 19.2 1.0 CE2 B:TYR109 4.6 23.9 1.0 CG B:GLU119 4.6 20.8 1.0 CE1 B:TYR125 4.6 35.5 1.0 CB B:GLU119 4.7 21.1 1.0 CZ B:TYR109 4.8 21.9 1.0

Y.S.Wang, B.Zhang, J.Zhu, C.L.Yang, Y.Guo, C.L.Liu, F.Liu, H.Huang, S.Zhao, Y.Liang, R.H.Jiao, R.X.Tan, H.M.Ge. Molecular Basis For the Final Oxidative Rearrangement Steps in Chartreusin Biosynthesis. J. Am. Chem. Soc. V. 140 10909 2018.
ISSN: ESSN 1520-5126
PubMed: 30067334
DOI: 10.1021/JACS.8B06623