Fluorine in PDB 6qhx: Time Resolved Structural Analysis of the Full Turnover of An Enzyme - 6156 Ms

All present enzymatic activity of Time Resolved Structural Analysis of the Full Turnover of An Enzyme - 6156 Ms:
3.8.1.3;

The structure of Time Resolved Structural Analysis of the Full Turnover of An Enzyme - 6156 Ms, PDB code: 6qhx was solved by E.C.Schulz, P.Mehrabi, E.F.Pai, D.Miller, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.97 / 1.85
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	41.700, 79.500, 84.450, 90.00, 103.20, 90.00
R / Rfree (%)	22.4 / 25.4

The binding sites of Fluorine atom in the Time Resolved Structural Analysis of the Full Turnover of An Enzyme - 6156 Ms (pdb code 6qhx). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 2 binding sites of Fluorine where determined in the Time Resolved Structural Analysis of the Full Turnover of An Enzyme - 6156 Ms, PDB code: 6qhx:
Jump to Fluorine binding site number: 1; 2;

Fluorine binding site 1 out of 2 in the Time Resolved Structural Analysis of the Full Turnover of An Enzyme - 6156 Ms


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Time Resolved Structural Analysis of the Full Turnover of An Enzyme - 6156 Ms within 5.0Å range: probe atom residue distance (Å) B Occ A:F401 b:33.5 occ:1.00 F A:FAH401 0.0 33.5 1.0 CH3 A:FAH401 1.4 32.8 1.0 C A:FAH401 2.4 33.9 1.0 O A:FAH401 2.6 37.3 1.0 O A:HOH662 3.0 38.4 1.0 CB A:ALA236 3.4 29.9 1.0 OXT A:FAH401 3.5 37.4 1.0 CA A:ALA236 3.8 26.0 1.0 O A:ALA236 4.0 30.5 1.0 C A:ALA236 4.4 31.2 1.0 O A:HOH549 4.7 37.3 1.0

Fluorine binding site 2 out of 2 in the Time Resolved Structural Analysis of the Full Turnover of An Enzyme - 6156 Ms


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Time Resolved Structural Analysis of the Full Turnover of An Enzyme - 6156 Ms within 5.0Å range: probe atom residue distance (Å) B Occ B:F401 b:30.1 occ:0.55 F B:FAH401 0.0 30.1 0.6 CH3 B:FAH401 1.3 27.9 0.6 C B:FAH401 2.3 30.1 0.6 OH B:TYR219 2.4 24.9 1.0 NE1 B:TRP156 2.6 24.7 1.0 CE2 B:TYR219 2.9 27.3 1.0 OXT B:FAH401 3.0 29.5 0.6 O B:FAH401 3.0 29.7 0.6 CZ B:TYR219 3.1 25.9 1.0 NE2 B:HIS155 3.1 29.2 1.0 CD1 B:TRP156 3.4 26.0 1.0 CE2 B:TRP156 3.4 26.7 1.0 NH1 B:ARG111 3.5 23.9 1.0 CD2 B:HIS155 3.7 22.7 1.0 CZ2 B:TRP156 3.9 27.5 1.0 CE1 B:HIS155 4.0 27.4 1.0 CD2 B:TYR219 4.2 21.3 1.0 CD B:ARG111 4.3 22.7 1.0 OD2 B:ASP110 4.4 22.4 1.0 CE1 B:TYR219 4.4 25.6 1.0 CZ B:ARG111 4.4 23.7 1.0 CG B:TRP156 4.4 23.1 1.0 CD2 B:TRP156 4.5 22.3 1.0 OD1 B:ASP110 4.6 21.6 1.0 NE B:ARG111 4.7 22.6 1.0 CG B:HIS155 4.8 21.4 1.0 CG B:ASP110 4.9 23.1 1.0 ND1 B:HIS155 4.9 26.4 1.0

P.Mehrabi, E.C.Schulz, R.Dsouza, H.M.Muller-Werkmeister, F.Tellkamp, R.J.D.Miller, E.F.Pai. Time-Resolved Crystallography Reveals Allosteric Communication Aligned with Molecular Breathing. Science V. 365 1167 2019.
ISSN: ESSN 1095-9203
PubMed: 31515393
DOI: 10.1126/SCIENCE.AAW9904