Fluorine in PDB 6qi1: Time Resolved Structural Analysis of the Full Turnover of An Enzyme - 12312 Ms

All present enzymatic activity of Time Resolved Structural Analysis of the Full Turnover of An Enzyme - 12312 Ms:
3.8.1.3;

The structure of Time Resolved Structural Analysis of the Full Turnover of An Enzyme - 12312 Ms, PDB code: 6qi1 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)	20.05 / 1.90
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	41.760, 79.610, 84.430, 90.00, 102.86, 90.00
R / Rfree (%)	21.2 / 25.9

The binding sites of Fluorine atom in the Time Resolved Structural Analysis of the Full Turnover of An Enzyme - 12312 Ms (pdb code 6qi1). 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 - 12312 Ms, PDB code: 6qi1:
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 - 12312 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 - 12312 Ms within 5.0Å range: probe atom residue distance (Å) B Occ A:F401 b:17.5 occ:0.45 F A:FAH401 0.0 17.5 0.5 CH3 A:FAH401 1.4 19.4 0.5 CH3 A:FAH401 1.8 18.8 0.4 C A:FAH401 2.4 18.4 0.5 O A:FAH401 2.5 19.8 0.4 C A:FAH401 2.5 18.4 0.4 O A:FAH401 2.7 19.7 0.5 NE1 A:TRP156 3.0 15.1 1.0 F A:FAH401 3.0 17.1 0.4 O A:HOH509 3.2 25.5 1.0 OXT A:FAH401 3.5 18.9 0.5 NE2 A:HIS155 3.6 18.1 1.0 CD1 A:ILE253 3.7 24.6 1.0 OXT A:FAH401 3.7 18.0 0.4 OD2 A:ASP110 3.8 17.9 1.0 CE2 A:TRP156 3.8 18.8 1.0 CD1 A:TRP156 4.0 18.6 1.0 CZ2 A:TRP156 4.0 18.4 1.0 CE1 A:HIS155 4.1 19.4 1.0 OH A:TYR219 4.3 20.1 1.0 CE2 A:TYR141 4.4 19.5 1.0 CG2 A:ILE253 4.5 22.8 1.0 CG A:ASP110 4.8 15.9 1.0 NH1 A:ARG114 4.8 20.4 1.0 CD2 A:HIS155 4.8 19.8 1.0 NE2 A:HIS280 4.9 17.3 1.0 CG1 A:ILE253 4.9 26.7 1.0 NH1 A:ARG111 5.0 16.7 1.0 CE1 A:HIS280 5.0 21.4 1.0 CG2 A:ILE153 5.0 21.6 1.0 CB A:ILE253 5.0 27.5 1.0

Fluorine binding site 2 out of 2 in the Time Resolved Structural Analysis of the Full Turnover of An Enzyme - 12312 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 - 12312 Ms within 5.0Å range: probe atom residue distance (Å) B Occ A:F401 b:17.1 occ:0.42 F A:FAH401 0.0 17.1 0.4 CH3 A:FAH401 1.4 18.8 0.4 CH3 A:FAH401 1.7 19.4 0.5 OXT A:FAH401 2.2 18.9 0.5 C A:FAH401 2.2 18.4 0.5 C A:FAH401 2.4 18.4 0.4 OXT A:FAH401 2.7 18.0 0.4 OH A:TYR141 3.0 27.6 1.0 NH1 A:ARG114 3.0 20.4 1.0 F A:FAH401 3.0 17.5 0.5 O A:FAH401 3.4 19.7 0.5 O A:FAH401 3.5 19.8 0.4 CE2 A:TYR141 3.6 19.5 1.0 O A:ASP134 3.6 17.3 1.0 CZ A:TYR141 3.6 21.0 1.0 CG2 A:ILE135 3.8 14.4 1.0 CE1 A:HIS280 3.8 21.4 1.0 OD2 A:ASP110 4.0 17.9 1.0 CZ A:ARG114 4.1 15.4 1.0 CG2 A:ILE253 4.3 22.8 1.0 NE A:ARG114 4.3 12.8 1.0 CA A:ILE135 4.4 18.0 1.0 CB A:ILE135 4.4 15.8 1.0 CB A:ILE253 4.4 27.5 1.0 NE2 A:HIS280 4.4 17.3 1.0 CZ2 A:TRP156 4.6 18.4 1.0 CD1 A:ILE253 4.6 24.6 1.0 C A:ASP134 4.7 16.1 1.0 ND1 A:HIS280 4.8 18.2 1.0 CA A:ASP110 4.8 12.8 1.0 CD2 A:TYR141 4.8 22.5 1.0 CG A:ASP110 4.8 15.9 1.0 CE1 A:TYR141 4.9 21.4 1.0 O A:HOH509 5.0 25.5 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