Fluorine in PDB 6bps: Crystal Structure of Cysteine-Bound Ferrous Form of the Uncrosslinked F2-TYR157 Human Cysteine Dioxygenase

All present enzymatic activity of Crystal Structure of Cysteine-Bound Ferrous Form of the Uncrosslinked F2-TYR157 Human Cysteine Dioxygenase:
1.13.11.20;

The structure of Crystal Structure of Cysteine-Bound Ferrous Form of the Uncrosslinked F2-TYR157 Human Cysteine Dioxygenase, PDB code: 6bps was solved by A.Liu, J.Li, I.Shin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	37.88 / 2.10
Space group	P 65
Cell size a, b, c (Å), α, β, γ (°)	131.210, 131.210, 34.144, 90.00, 90.00, 120.00
R / Rfree (%)	16.7 / 20.3

The structure of Crystal Structure of Cysteine-Bound Ferrous Form of the Uncrosslinked F2-TYR157 Human Cysteine Dioxygenase also contains other interesting chemical elements:

Iron

(Fe)

1 atom

The binding sites of Fluorine atom in the Crystal Structure of Cysteine-Bound Ferrous Form of the Uncrosslinked F2-TYR157 Human Cysteine Dioxygenase (pdb code 6bps). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 2 binding sites of Fluorine where determined in the Crystal Structure of Cysteine-Bound Ferrous Form of the Uncrosslinked F2-TYR157 Human Cysteine Dioxygenase, PDB code: 6bps:
Jump to Fluorine binding site number: 1; 2;

Fluorine binding site 1 out of 2 in the Crystal Structure of Cysteine-Bound Ferrous Form of the Uncrosslinked F2-TYR157 Human Cysteine Dioxygenase


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Crystal Structure of Cysteine-Bound Ferrous Form of the Uncrosslinked F2-TYR157 Human Cysteine Dioxygenase within 5.0Å range: probe atom residue distance (Å) B Occ A:F157 b:43.4 occ:1.00 F1 A:F2Y157 0.0 43.4 1.0 CE1 A:F2Y157 1.3 34.1 1.0 SG A:CYS93 2.2 24.6 0.3 CZ A:F2Y157 2.3 30.8 1.0 CD1 A:F2Y157 2.4 26.8 1.0 OH A:F2Y157 2.7 35.0 1.0 O A:HOH499 3.0 37.8 1.0 CB A:CYS93 3.4 25.2 0.7 CB A:CYS93 3.4 25.1 0.3 ND1 A:HIS155 3.5 23.0 1.0 CE2 A:F2Y157 3.6 38.2 1.0 CG A:F2Y157 3.6 24.6 1.0 SG A:CYS93 3.7 29.3 0.7 CB A:HIS155 3.8 16.6 1.0 O A:PHE94 3.9 18.2 1.0 CA A:CYS93 3.9 20.8 0.3 CA A:CYS93 3.9 20.8 0.7 CG A:HIS155 4.1 21.7 1.0 CD2 A:F2Y157 4.1 31.7 1.0 O A:LEU156 4.1 20.9 1.0 N A:PHE94 4.1 20.1 1.0 C A:CYS93 4.2 19.8 1.0 N A:CYS302 4.4 28.9 1.0 C A:LEU156 4.5 18.0 1.0 N A:LEU156 4.5 18.2 1.0 C A:PHE94 4.5 18.8 1.0 CA A:HIS155 4.6 14.8 1.0 CE1 A:HIS155 4.6 21.3 1.0 F2 A:F2Y157 4.7 46.2 1.0 CD2 A:HIS88 4.7 21.4 1.0 C A:HIS155 4.8 19.2 1.0 CB A:F2Y157 4.9 20.8 1.0 N A:F2Y157 4.9 20.6 1.0

Fluorine binding site 2 out of 2 in the Crystal Structure of Cysteine-Bound Ferrous Form of the Uncrosslinked F2-TYR157 Human Cysteine Dioxygenase


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Crystal Structure of Cysteine-Bound Ferrous Form of the Uncrosslinked F2-TYR157 Human Cysteine Dioxygenase within 5.0Å range: probe atom residue distance (Å) B Occ A:F157 b:46.2 occ:1.00 F2 A:F2Y157 0.0 46.2 1.0 CE2 A:F2Y157 1.3 38.2 1.0 CD2 A:F2Y157 2.3 31.7 1.0 CZ A:F2Y157 2.4 30.8 1.0 NH1 A:ARG60 2.4 40.2 1.0 OH A:F2Y157 2.8 35.0 1.0 O A:CYS302 3.1 31.0 1.0 CE A:MET73 3.4 31.2 1.0 SD A:MET73 3.5 28.4 1.0 CG A:F2Y157 3.6 24.6 1.0 CE1 A:F2Y157 3.6 34.1 1.0 CZ A:ARG60 3.7 46.7 1.0 CE A:MET179 3.7 38.2 1.0 O A:HOH484 3.9 42.6 1.0 CD1 A:F2Y157 4.1 26.8 1.0 CZ A:PHE161 4.2 21.3 1.0 C A:CYS302 4.3 29.6 1.0 O A:HOH481 4.3 34.3 1.0 NE A:ARG60 4.3 27.6 1.0 CE1 A:PHE161 4.5 23.3 1.0 N A:CYS302 4.5 28.9 1.0 NH2 A:ARG60 4.7 36.1 1.0 CE2 A:PHE161 4.7 22.4 1.0 F1 A:F2Y157 4.7 43.4 1.0 CB A:F2Y157 4.8 20.8 1.0 CG A:MET73 4.9 24.2 1.0 O A:PHE161 4.9 28.9 1.0

J.Li, W.P.Griffith, I.Davis, I.Shin, J.Wang, F.Li, Y.Wang, D.J.Wherritt, A.Liu. Cleavage of A Carbon-Fluorine Bond By An Engineered Cysteine Dioxygenase. Nat. Chem. Biol. V. 14 853 2018.
ISSN: ESSN 1552-4469
PubMed: 29942080
DOI: 10.1038/S41589-018-0085-5