Iron in PDB 7kqs: A 1.68-A Resolution 3-Fluoro-L-Tyrosine Bound Crystal Structure of Heme-Dependent Tyrosine Hydroxylase

The structure of A 1.68-A Resolution 3-Fluoro-L-Tyrosine Bound Crystal Structure of Heme-Dependent Tyrosine Hydroxylase, PDB code: 7kqs was solved by Y.Wang, A.Liu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.40 / 1.68
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	47.526, 129.719, 48.533, 90, 94.19, 90
R / Rfree (%)	17.3 / 20.3

The structure of A 1.68-A Resolution 3-Fluoro-L-Tyrosine Bound Crystal Structure of Heme-Dependent Tyrosine Hydroxylase also contains other interesting chemical elements:

Fluorine

(F)

4 atoms

The binding sites of Iron atom in the A 1.68-A Resolution 3-Fluoro-L-Tyrosine Bound Crystal Structure of Heme-Dependent Tyrosine Hydroxylase (pdb code 7kqs). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the A 1.68-A Resolution 3-Fluoro-L-Tyrosine Bound Crystal Structure of Heme-Dependent Tyrosine Hydroxylase, PDB code: 7kqs:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the A 1.68-A Resolution 3-Fluoro-L-Tyrosine Bound Crystal Structure of Heme-Dependent Tyrosine Hydroxylase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of A 1.68-A Resolution 3-Fluoro-L-Tyrosine Bound Crystal Structure of Heme-Dependent Tyrosine Hydroxylase within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe401 b:29.0 occ:1.00 FE A:HEM401 0.0 29.0 1.0 NC A:HEM401 2.0 20.9 1.0 NB A:HEM401 2.0 17.9 1.0 ND A:HEM401 2.1 27.6 1.0 NA A:HEM401 2.1 24.4 1.0 NE2 A:HIS196 2.4 32.1 1.0 C1C A:HEM401 3.0 24.1 1.0 C4B A:HEM401 3.0 25.0 1.0 C4C A:HEM401 3.1 23.6 1.0 C4D A:HEM401 3.1 30.5 1.0 C1B A:HEM401 3.1 21.8 1.0 C1A A:HEM401 3.1 27.4 1.0 C1D A:HEM401 3.1 26.3 1.0 C4A A:HEM401 3.1 24.4 1.0 CE1 A:HIS196 3.1 40.3 1.0 O A:HOH560 3.3 30.5 1.0 CHC A:HEM401 3.3 23.6 1.0 CHA A:HEM401 3.4 28.9 1.0 CHD A:HEM401 3.5 26.4 1.0 CHB A:HEM401 3.5 31.5 1.0 CD2 A:HIS196 3.6 32.4 1.0 C2C A:HEM401 4.2 23.1 1.0 C3B A:HEM401 4.2 25.0 1.0 C3C A:HEM401 4.3 25.8 1.0 C2B A:HEM401 4.3 23.9 1.0 C3D A:HEM401 4.3 30.1 1.0 C2D A:HEM401 4.3 32.2 1.0 N A:YOF404 4.3 22.5 0.3 C2A A:HEM401 4.3 21.8 1.0 C3A A:HEM401 4.3 23.1 1.0 ND1 A:HIS196 4.4 42.3 1.0 N A:YOF404 4.4 22.3 0.7 CG A:HIS196 4.6 32.4 1.0 CD2 A:YOF404 4.9 19.7 0.7 CE2 A:YOF404 4.9 19.9 0.7

Iron binding site 2 out of 2 in the A 1.68-A Resolution 3-Fluoro-L-Tyrosine Bound Crystal Structure of Heme-Dependent Tyrosine Hydroxylase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of A 1.68-A Resolution 3-Fluoro-L-Tyrosine Bound Crystal Structure of Heme-Dependent Tyrosine Hydroxylase within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe401 b:30.8 occ:1.00 FE B:HEM401 0.0 30.8 1.0 NB B:HEM401 2.0 23.2 1.0 NC B:HEM401 2.0 28.7 1.0 ND B:HEM401 2.0 27.5 1.0 NA B:HEM401 2.1 28.3 1.0 NE2 B:HIS196 2.5 36.8 1.0 C4B B:HEM401 3.0 32.1 1.0 C1C B:HEM401 3.0 28.1 1.0 C1B B:HEM401 3.1 27.2 1.0 C4D B:HEM401 3.1 32.5 1.0 C1D B:HEM401 3.1 30.6 1.0 C4C B:HEM401 3.1 27.6 1.0 CE1 B:HIS196 3.1 44.5 1.0 C1A B:HEM401 3.1 29.5 1.0 C4A B:HEM401 3.2 25.5 1.0 CHC B:HEM401 3.3 26.8 1.0 O B:HOH540 3.4 30.0 1.0 CHD B:HEM401 3.5 31.7 1.0 CHA B:HEM401 3.5 27.1 1.0 CHB B:HEM401 3.5 29.8 1.0 CD2 B:HIS196 3.7 33.7 1.0 C2C B:HEM401 4.2 30.4 1.0 C3B B:HEM401 4.2 25.7 1.0 C2B B:HEM401 4.2 26.3 1.0 C3C B:HEM401 4.3 34.6 1.0 N B:YOF402 4.3 24.7 0.3 C3D B:HEM401 4.3 35.0 1.0 C2D B:HEM401 4.3 35.0 1.0 C2A B:HEM401 4.3 27.2 1.0 ND1 B:HIS196 4.4 40.7 1.0 C3A B:HEM401 4.4 25.8 1.0 N B:YOF402 4.4 24.5 0.7 CG B:HIS196 4.7 34.1 1.0 CD2 B:YOF402 4.9 21.8 0.7 CE2 B:YOF402 4.9 19.6 0.7

Y.Wang, I.Davis, I.Shin, H.Xu, A.Liu. Molecular Rationale For Partitioning Between C-H and C-F Bond Activation in Heme-Dependent Tyrosine Hydroxylase. J.Am.Chem.Soc. 2021.
ISSN: ESSN 1520-5126
PubMed: 33734681
DOI: 10.1021/JACS.1C00175