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Fluorine in PDB 6qhv: Time Resolved Structural Analysis of the Full Turnover of An Enzyme - 100 Ms

Enzymatic activity of Time Resolved Structural Analysis of the Full Turnover of An Enzyme - 100 Ms

All present enzymatic activity of Time Resolved Structural Analysis of the Full Turnover of An Enzyme - 100 Ms:
3.8.1.3;

Protein crystallography data

The structure of Time Resolved Structural Analysis of the Full Turnover of An Enzyme - 100 Ms, PDB code: 6qhv 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) 20.00 / 1.72
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 41.370, 78.580, 83.550, 90.00, 102.73, 90.00
R / Rfree (%) 16.1 / 19.4

Fluorine Binding Sites:

The binding sites of Fluorine atom in the Time Resolved Structural Analysis of the Full Turnover of An Enzyme - 100 Ms (pdb code 6qhv). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total only one binding site of Fluorine was determined in the Time Resolved Structural Analysis of the Full Turnover of An Enzyme - 100 Ms, PDB code: 6qhv:

Fluorine binding site 1 out of 1 in 6qhv

Go back to Fluorine Binding Sites List in 6qhv
Fluorine binding site 1 out of 1 in the Time Resolved Structural Analysis of the Full Turnover of An Enzyme - 100 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 - 100 Ms within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F401

b:28.5
occ:1.00
F A:FAH401 0.0 28.5 1.0
CH3 A:FAH401 1.5 22.4 1.0
C A:FAH401 2.6 25.1 1.0
NE1 A:TRP156 2.7 12.4 1.0
O A:HOH513 2.7 26.5 1.0
NE2 A:HIS155 2.8 13.8 1.0
O A:FAH401 2.9 20.6 1.0
OH A:TYR219 3.0 18.2 1.0
CD1 A:TRP156 3.6 14.2 1.0
CE1 A:HIS155 3.7 16.1 1.0
OXT A:FAH401 3.7 26.6 1.0
CE2 A:TRP156 3.7 13.4 1.0
CD2 A:HIS155 3.8 14.9 1.0
OD1 A:ASP110 3.9 15.9 1.0
CZ A:TYR219 4.0 14.5 1.0
CZ2 A:TRP156 4.1 14.8 1.0
CE2 A:TYR219 4.2 18.6 1.0
CD1 A:ILE253 4.3 18.9 1.0
NH1 A:ARG111 4.3 14.2 1.0
CH2 A:TRP185 4.6 22.1 1.0
O A:HOH509 4.7 21.6 1.0
CG A:ASP110 4.8 12.3 1.0
OD2 A:ASP110 4.8 11.7 1.0
CG A:TRP156 4.8 11.2 1.0
ND1 A:HIS155 4.9 15.2 1.0
CZ2 A:TRP185 4.9 19.9 1.0
CD2 A:TRP156 4.9 10.4 1.0
CG A:HIS155 4.9 13.0 1.0

Reference:

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
Page generated: Fri Aug 2 00:52:01 2024

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