Iron in PDB 7y3x: Crystal Structure of BTG13 Mutant (H58F)

The structure of Crystal Structure of BTG13 Mutant (H58F), PDB code: 7y3x was solved by X.D.Hou, Y.J.Rao, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	79.01 / 2.14
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	79.292, 99.742, 129.435, 90, 90, 90
R / Rfree (%)	17.4 / 21

The binding sites of Iron atom in the Crystal Structure of BTG13 Mutant (H58F) (pdb code 7y3x). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Crystal Structure of BTG13 Mutant (H58F), PDB code: 7y3x:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Crystal Structure of BTG13 Mutant (H58F)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structure of BTG13 Mutant (H58F) within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:24.3 occ:1.00 OQ2 A:KCX377 2.0 28.2 1.0 NE2 A:HIS296 2.1 26.6 1.0 NE2 A:HIS374 2.1 23.8 1.0 NE2 A:HIS55 2.2 23.0 1.0 NE2 A:HIS158 2.2 28.8 1.0 O A:HOH760 2.3 18.8 1.0 CE1 A:HIS158 3.0 27.2 1.0 CE1 A:HIS296 3.0 33.2 1.0 CD2 A:HIS296 3.1 27.4 1.0 CD2 A:HIS374 3.1 24.3 1.0 CD2 A:HIS55 3.1 26.4 1.0 CX A:KCX377 3.2 31.8 1.0 CE1 A:HIS374 3.2 28.4 1.0 CE1 A:HIS55 3.2 26.6 1.0 CD2 A:HIS158 3.3 28.3 1.0 OQ1 A:KCX377 3.7 29.0 1.0 NZ A:KCX377 4.1 36.4 1.0 ND1 A:HIS296 4.2 27.1 1.0 CG A:HIS296 4.2 26.5 1.0 ND1 A:HIS158 4.2 28.1 1.0 O A:HOH798 4.2 31.5 1.0 CG A:HIS374 4.3 25.2 1.0 ND1 A:HIS374 4.3 26.6 1.0 CG A:HIS55 4.3 26.4 1.0 ND1 A:HIS55 4.3 25.1 1.0 CG A:HIS158 4.4 29.2 1.0 O A:HOH601 4.5 30.0 1.0 CE A:KCX377 5.0 37.6 1.0 CZ A:PHE292 5.0 27.3 1.0

Iron binding site 2 out of 2 in the Crystal Structure of BTG13 Mutant (H58F)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Crystal Structure of BTG13 Mutant (H58F) within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe501 b:25.5 occ:1.00 OQ1 B:KCX377 2.0 29.3 1.0 NE2 B:HIS296 2.0 25.1 1.0 NE2 B:HIS158 2.1 24.9 1.0 NE2 B:HIS55 2.1 26.6 1.0 NE2 B:HIS374 2.2 25.2 1.0 O B:HOH742 2.2 17.8 1.0 CE1 B:HIS158 3.0 26.3 1.0 CE1 B:HIS296 3.0 27.2 1.0 CD2 B:HIS296 3.1 27.8 1.0 CE1 B:HIS55 3.1 27.9 1.0 CE1 B:HIS374 3.1 26.2 1.0 CD2 B:HIS55 3.1 26.7 1.0 CD2 B:HIS158 3.1 31.1 1.0 CX B:KCX377 3.2 32.1 1.0 CD2 B:HIS374 3.2 26.7 1.0 OQ2 B:KCX377 3.7 32.1 1.0 ND1 B:HIS158 4.1 23.4 1.0 ND1 B:HIS296 4.2 24.2 1.0 NZ B:KCX377 4.2 33.5 1.0 CG B:HIS296 4.2 25.5 1.0 ND1 B:HIS55 4.2 28.4 1.0 CG B:HIS158 4.2 28.3 1.0 ND1 B:HIS374 4.2 23.7 1.0 CG B:HIS55 4.3 26.9 1.0 O B:HOH773 4.3 34.2 1.0 CG B:HIS374 4.3 25.9 1.0 O B:HOH612 4.4 29.1 1.0 CZ B:PHE292 4.9 28.8 1.0 CE B:KCX377 5.0 34.9 1.0

X.Hou, H.Xu, Z.Deng, Y.Yan, Z.Yuan, X.Liu, Z.Su, S.Yang, Y.Zhang, Y.Rao. Discovery of the Biosynthetic Pathway of Beticolin 1 Reveals A Novel Non-Heme Iron-Dependent Oxygenase For Anthraquinone Ring Cleavage. Angew.Chem.Int.Ed.Engl. V. 61 08772 2022.
ISSN: ESSN 1521-3773
PubMed: 35862137
DOI: 10.1002/ANIE.202208772