Fluorine in PDB 6dz5: Citrobacter Freundii Tyrosine Phenol-Lyase F448A Mutant Complexed with L-Alanine

All present enzymatic activity of Citrobacter Freundii Tyrosine Phenol-Lyase F448A Mutant Complexed with L-Alanine:
4.1.99.2;

The structure of Citrobacter Freundii Tyrosine Phenol-Lyase F448A Mutant Complexed with L-Alanine, PDB code: 6dz5 was solved by R.S.Phillips, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	44.47 / 2.26
Space group	P 2 21 21
Cell size a, b, c (Å), α, β, γ (°)	59.880, 132.810, 145.370, 90.00, 90.00, 90.00
R / Rfree (%)	18.3 / 22.1

The structure of Citrobacter Freundii Tyrosine Phenol-Lyase F448A Mutant Complexed with L-Alanine also contains other interesting chemical elements:

Potassium

(K)

2 atoms

The binding sites of Fluorine atom in the Citrobacter Freundii Tyrosine Phenol-Lyase F448A Mutant Complexed with L-Alanine (pdb code 6dz5). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 2 binding sites of Fluorine where determined in the Citrobacter Freundii Tyrosine Phenol-Lyase F448A Mutant Complexed with L-Alanine, PDB code: 6dz5:
Jump to Fluorine binding site number: 1; 2;

Fluorine binding site 1 out of 2 in the Citrobacter Freundii Tyrosine Phenol-Lyase F448A Mutant Complexed with L-Alanine


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Citrobacter Freundii Tyrosine Phenol-Lyase F448A Mutant Complexed with L-Alanine within 5.0Å range: probe atom residue distance (Å) B Occ A:F502 b:96.3 occ:1.00 F A:P61502 0.0 96.3 1.0 CE1 A:P61502 1.3 95.9 1.0 CZ A:P61502 2.3 96.4 1.0 CD1 A:P61502 2.4 92.2 1.0 OH A:P61502 2.6 0.9 1.0 NH2 A:ARG381 3.1 0.5 1.0 CG A:P61502 3.6 84.6 1.0 CE2 A:P61502 3.6 90.8 1.0 CE1 A:PHE449 3.7 96.6 1.0 CE A:MET379 3.8 63.0 1.0 CZ A:PHE449 3.9 98.0 1.0 CZ A:PHE36 4.0 60.2 1.0 CD2 A:P61502 4.1 89.5 1.0 SD A:MET379 4.1 69.3 1.0 CZ A:ARG381 4.3 93.1 1.0 CE1 A:PHE36 4.7 59.3 1.0 CE2 B:TYR71 4.7 56.6 1.0 O A:P61502 4.8 63.9 1.0 NH1 A:ARG381 4.8 77.5 1.0 CB A:P61502 4.9 75.5 1.0 CE2 A:PHE36 4.9 65.7 1.0

Fluorine binding site 2 out of 2 in the Citrobacter Freundii Tyrosine Phenol-Lyase F448A Mutant Complexed with L-Alanine


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Citrobacter Freundii Tyrosine Phenol-Lyase F448A Mutant Complexed with L-Alanine within 5.0Å range: probe atom residue distance (Å) B Occ B:F601 b:85.6 occ:1.00 F B:P61601 0.0 85.6 1.0 CE1 B:P61601 1.4 98.2 1.0 CD1 B:P61601 2.4 96.2 1.0 CZ B:P61601 2.4 0.4 1.0 OH B:P61601 2.9 0.5 1.0 CE2 B:P61601 3.7 92.8 1.0 CG B:P61601 3.7 92.7 1.0 CE B:MET379 3.7 69.4 1.0 NH2 B:ARG381 3.9 63.7 0.4 CE2 A:TYR71 4.1 76.2 1.0 CZ B:PHE36 4.1 52.5 1.0 CD2 B:P61601 4.1 96.7 1.0 CE1 B:PHE449 4.2 68.8 1.0 O A:HOH670 4.2 76.3 1.0 CZ B:PHE449 4.3 73.7 1.0 SD B:MET379 4.4 61.9 1.0 OXT B:P61601 4.5 70.9 1.0 O B:HOH766 4.7 56.9 1.0 OH A:TYR71 4.7 96.3 1.0 CE1 B:PHE36 4.8 56.3 1.0 CZ A:TYR71 4.9 82.1 1.0 CD2 A:TYR71 4.9 73.9 1.0 CB B:P61601 4.9 84.9 1.0

R.S.Phillips, S.Craig. Crystal Structures of Wild-Type and F448A Mutant Citrobacter Freundii Tyrosine Phenol-Lyase Complexed with A Substrate and Inhibitors: Implications For the Reaction Mechanism. Biochemistry V. 57 6166 2018.
ISSN: ISSN 1520-4995
PubMed: 30260636
DOI: 10.1021/ACS.BIOCHEM.8B00724