Iron in PDB 7kqt: A 1.84-A Resolution Crystal Structure of Heme-Dependent L-Tyrosine Hydroxylase in Complex with 3-Fluoro-L-Tyrosine and Cyanide

The structure of A 1.84-A Resolution Crystal Structure of Heme-Dependent L-Tyrosine Hydroxylase in Complex with 3-Fluoro-L-Tyrosine and Cyanide, PDB code: 7kqt 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)	48.27 / 1.84
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	47.375, 129.446, 48.401, 90, 94.29, 90
R / Rfree (%)	20.3 / 25

The structure of A 1.84-A Resolution Crystal Structure of Heme-Dependent L-Tyrosine Hydroxylase in Complex with 3-Fluoro-L-Tyrosine and Cyanide also contains other interesting chemical elements:

Fluorine

(F)

4 atoms

The binding sites of Iron atom in the A 1.84-A Resolution Crystal Structure of Heme-Dependent L-Tyrosine Hydroxylase in Complex with 3-Fluoro-L-Tyrosine and Cyanide (pdb code 7kqt). 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 1.84-A Resolution Crystal Structure of Heme-Dependent L-Tyrosine Hydroxylase in Complex with 3-Fluoro-L-Tyrosine and Cyanide, PDB code: 7kqt:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the A 1.84-A Resolution Crystal Structure of Heme-Dependent L-Tyrosine Hydroxylase in Complex with 3-Fluoro-L-Tyrosine and Cyanide


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of A 1.84-A Resolution Crystal Structure of Heme-Dependent L-Tyrosine Hydroxylase in Complex with 3-Fluoro-L-Tyrosine and Cyanide within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe401 b:41.6 occ:1.00 FE A:HEM401 0.0 41.6 1.0 C A:CYN403 2.0 50.2 1.0 NB A:HEM401 2.0 28.6 1.0 NC A:HEM401 2.0 36.4 1.0 NA A:HEM401 2.1 34.8 1.0 ND A:HEM401 2.1 39.4 1.0 NE2 A:HIS196 2.5 57.5 1.0 C1C A:HEM401 3.0 34.0 1.0 C4B A:HEM401 3.0 32.5 1.0 C1A A:HEM401 3.1 44.4 1.0 C4D A:HEM401 3.1 50.4 1.0 N A:CYN403 3.1 46.4 1.0 C1B A:HEM401 3.1 33.5 1.0 C4A A:HEM401 3.1 30.6 1.0 C4C A:HEM401 3.1 30.2 1.0 C1D A:HEM401 3.2 41.5 1.0 CE1 A:HIS196 3.2 54.4 1.0 CHC A:HEM401 3.3 29.9 1.0 CHA A:HEM401 3.5 47.9 1.0 CHB A:HEM401 3.5 40.3 1.0 CD2 A:HIS196 3.6 58.6 1.0 CHD A:HEM401 3.6 37.0 1.0 C3B A:HEM401 4.2 30.2 1.0 C2C A:HEM401 4.2 35.2 1.0 C2B A:HEM401 4.3 32.3 1.0 C2A A:HEM401 4.3 42.6 1.0 C3C A:HEM401 4.3 33.9 1.0 C3D A:HEM401 4.3 51.1 1.0 C3A A:HEM401 4.3 34.2 1.0 C2D A:HEM401 4.3 50.0 1.0 ND1 A:HIS196 4.4 49.8 1.0 CG A:HIS196 4.6 52.8 1.0 N A:YOF402 5.0 26.3 0.7

Iron binding site 2 out of 2 in the A 1.84-A Resolution Crystal Structure of Heme-Dependent L-Tyrosine Hydroxylase in Complex with 3-Fluoro-L-Tyrosine and Cyanide


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of A 1.84-A Resolution Crystal Structure of Heme-Dependent L-Tyrosine Hydroxylase in Complex with 3-Fluoro-L-Tyrosine and Cyanide within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe401 b:36.2 occ:1.00 FE B:HEM401 0.0 36.2 1.0 C B:CYN403 1.9 36.9 1.0 NB B:HEM401 2.0 25.1 1.0 ND B:HEM401 2.1 34.4 1.0 NA B:HEM401 2.1 26.9 1.0 NC B:HEM401 2.1 35.4 1.0 NE2 B:HIS196 2.5 47.7 1.0 N B:CYN403 3.0 36.5 1.0 C4B B:HEM401 3.0 31.6 1.0 C1C B:HEM401 3.0 41.8 1.0 C4D B:HEM401 3.1 37.6 1.0 C1D B:HEM401 3.1 34.4 1.0 C1A B:HEM401 3.1 39.2 1.0 C1B B:HEM401 3.1 32.1 1.0 C4C B:HEM401 3.1 37.9 1.0 C4A B:HEM401 3.1 28.3 1.0 CE1 B:HIS196 3.2 45.1 1.0 CHC B:HEM401 3.4 31.4 1.0 CHA B:HEM401 3.5 37.9 1.0 CHD B:HEM401 3.5 35.6 1.0 CHB B:HEM401 3.6 27.8 1.0 CD2 B:HIS196 3.6 44.1 1.0 C2C B:HEM401 4.2 46.5 1.0 C3B B:HEM401 4.3 33.5 1.0 C3D B:HEM401 4.3 40.9 1.0 C2D B:HEM401 4.3 37.6 1.0 C3C B:HEM401 4.3 43.9 1.0 C2B B:HEM401 4.3 30.7 1.0 C2A B:HEM401 4.3 40.0 1.0 C3A B:HEM401 4.3 31.9 1.0 ND1 B:HIS196 4.4 41.7 1.0 CG B:HIS196 4.6 37.4 1.0

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