Fluorine in PDB 6qhw: Time Resolved Structural Analysis of the Full Turnover of An Enzyme - 4512 Ms

All present enzymatic activity of Time Resolved Structural Analysis of the Full Turnover of An Enzyme - 4512 Ms:
3.8.1.3;

The structure of Time Resolved Structural Analysis of the Full Turnover of An Enzyme - 4512 Ms, PDB code: 6qhw 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)	19.99 / 1.72
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	41.360, 78.660, 83.570, 90.00, 102.70, 90.00
R / Rfree (%)	18.5 / 22.6

The binding sites of Fluorine atom in the Time Resolved Structural Analysis of the Full Turnover of An Enzyme - 4512 Ms (pdb code 6qhw). 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 - 4512 Ms, PDB code: 6qhw:
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 - 4512 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 - 4512 Ms within 5.0Å range: probe atom residue distance (Å) B Occ B:F401 b:24.2 occ:0.50 F B:FAH401 0.0 24.2 0.5 CH3 B:FAH401 0.9 23.3 0.5 CH3 B:FAH401 1.4 23.1 0.5 F B:FAH401 1.9 22.7 0.5 C B:FAH401 2.3 25.0 0.5 O B:HOH511 2.4 30.4 1.0 C B:FAH401 2.4 24.2 0.5 OXT B:FAH401 2.7 20.0 0.5 NE2 B:HIS155 2.9 15.2 1.0 OXT B:FAH401 3.0 19.3 0.5 NE1 B:TRP156 3.0 16.1 1.0 O B:HOH543 3.0 33.4 1.0 OH B:TYR219 3.2 16.7 1.0 O B:FAH401 3.3 23.7 0.5 O B:FAH401 3.5 21.9 0.5 OD1 B:ASP110 3.5 20.3 1.0 CE1 B:HIS155 3.7 19.2 1.0 CD1 B:TRP156 3.9 14.6 1.0 CE2 B:TRP156 4.0 14.4 1.0 CD2 B:HIS155 4.0 14.6 1.0 CZ B:TYR219 4.2 18.8 1.0 CE1 B:TYR219 4.3 15.8 1.0 CZ2 B:TRP156 4.3 17.4 1.0 NH1 B:ARG111 4.3 17.4 1.0 CG B:ASP110 4.3 15.8 1.0 OD2 B:ASP110 4.4 12.9 1.0 CH2 B:TRP185 4.6 27.2 1.0 ND1 B:HIS155 4.9 15.9 1.0 CZ3 B:TRP185 5.0 30.4 1.0 CZ2 B:TRP185 5.0 28.4 1.0

Fluorine binding site 2 out of 2 in the Time Resolved Structural Analysis of the Full Turnover of An Enzyme - 4512 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 - 4512 Ms within 5.0Å range: probe atom residue distance (Å) B Occ B:F401 b:22.7 occ:0.50 F B:FAH401 0.0 22.7 0.5 CH3 B:FAH401 1.3 23.1 0.5 CH3 B:FAH401 1.5 23.3 0.5 F B:FAH401 1.9 24.2 0.5 C B:FAH401 2.5 25.0 0.5 O B:FAH401 2.7 23.7 0.5 C B:FAH401 2.9 24.2 0.5 O B:HOH543 3.0 33.4 1.0 NE1 B:TRP156 3.2 16.1 1.0 O B:FAH401 3.5 21.9 0.5 OXT B:FAH401 3.6 19.3 0.5 NE2 B:HIS155 3.6 15.2 1.0 OXT B:FAH401 3.7 20.0 0.5 CE1 B:HIS155 3.7 19.2 1.0 CG2 B:ILE153 3.9 23.2 0.8 CG2 B:ILE153 3.9 23.1 0.2 CE2 B:TYR141 3.9 30.6 1.0 O B:HOH511 4.0 30.4 1.0 CE2 B:TRP156 4.0 14.4 1.0 CD1 B:TRP156 4.1 14.6 1.0 CZ2 B:TRP156 4.3 17.4 1.0 OD1 B:ASP110 4.4 20.3 1.0 OH B:TYR141 4.7 32.9 1.0 CD2 B:TYR141 4.7 31.9 1.0 NH1 B:ARG114 4.8 13.7 1.0 CB B:ILE153 4.8 16.6 0.2 CB B:ILE153 4.8 16.5 0.8 CZ B:TYR141 4.8 28.5 1.0 CD2 B:HIS155 5.0 14.6 1.0 ND1 B:HIS155 5.0 15.9 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