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Fluorine in PDB 6qi0: Time Resolved Structural Analysis of the Full Turnover of An Enzyme - 9024 Ms

Enzymatic activity of Time Resolved Structural Analysis of the Full Turnover of An Enzyme - 9024 Ms

All present enzymatic activity of Time Resolved Structural Analysis of the Full Turnover of An Enzyme - 9024 Ms:
3.8.1.3;

Protein crystallography data

The structure of Time Resolved Structural Analysis of the Full Turnover of An Enzyme - 9024 Ms, PDB code: 6qi0 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 / 1.73
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 41.350, 78.570, 83.540, 90.00, 102.84, 90.00
R / Rfree (%) 16.9 / 19.9

Other elements in 6qi0:

The structure of Time Resolved Structural Analysis of the Full Turnover of An Enzyme - 9024 Ms also contains other interesting chemical elements:

Calcium (Ca) 1 atom

Fluorine Binding Sites:

The binding sites of Fluorine atom in the Time Resolved Structural Analysis of the Full Turnover of An Enzyme - 9024 Ms (pdb code 6qi0). 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 - 9024 Ms, PDB code: 6qi0:

Fluorine binding site 1 out of 1 in 6qi0

Go back to Fluorine Binding Sites List in 6qi0
Fluorine binding site 1 out of 1 in the Time Resolved Structural Analysis of the Full Turnover of An Enzyme - 9024 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 - 9024 Ms within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F401

b:27.9
occ:1.00
 F A:FAH401 0.0 27.9 1.0
CH3 A:FAH401 1.4 21.5 1.0
C A:FAH401 2.5 25.6 1.0
NE1 A:TRP156 2.6 15.9 1.0
O A:FAH401 2.8 26.7 1.0
NE2 A:HIS155 2.9 16.2 1.0
OH A:TYR219 3.1 17.5 1.0
CD1 A:TRP156 3.5 14.9 1.0
OXT A:FAH401 3.6 29.7 1.0
CE2 A:TRP156 3.6 15.2 1.0
CE1 A:HIS155 3.7 17.6 1.0
CD2 A:HIS155 3.8 15.1 1.0
OD1 A:ASP110 3.9 16.7 1.0
CZ2 A:TRP156 4.0 14.3 1.0
CZ A:TYR219 4.1 14.8 1.0
CE1 A:TYR219 4.1 18.2 1.0
NH1 A:ARG111 4.3 15.7 1.0
CD1 A:ILE253 4.5 22.9 1.0
CH2 A:TRP185 4.6 22.0 1.0
O A:HOH508 4.6 23.8 1.0
CG A:TRP156 4.7 12.6 1.0
CG A:ASP110 4.8 11.9 1.0
CD2 A:TRP156 4.8 11.3 1.0
OD2 A:ASP110 4.9 10.2 1.0
ND1 A:HIS155 4.9 15.8 1.0
CZ2 A:TRP185 5.0 21.5 1.0
CG A:HIS155 5.0 13.3 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: Tue Jul 15 15:05:02 2025

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