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Fluorine in PDB 6qhp: Time Resolved Structural Analysis of the Full Turnover of An Enzyme - 2256 Ms Covalent Intermediate 1

Enzymatic activity of Time Resolved Structural Analysis of the Full Turnover of An Enzyme - 2256 Ms Covalent Intermediate 1

All present enzymatic activity of Time Resolved Structural Analysis of the Full Turnover of An Enzyme - 2256 Ms Covalent Intermediate 1:
3.8.1.3;

Protein crystallography data

The structure of Time Resolved Structural Analysis of the Full Turnover of An Enzyme - 2256 Ms Covalent Intermediate 1, PDB code: 6qhp 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) 19.92 / 1.80
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 41.400, 78.670, 83.590, 90.00, 102.73, 90.00
R / Rfree (%) 21.8 / 26.6

Fluorine Binding Sites:

The binding sites of Fluorine atom in the Time Resolved Structural Analysis of the Full Turnover of An Enzyme - 2256 Ms Covalent Intermediate 1 (pdb code 6qhp). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 4 binding sites of Fluorine where determined in the Time Resolved Structural Analysis of the Full Turnover of An Enzyme - 2256 Ms Covalent Intermediate 1, PDB code: 6qhp:
Jump to Fluorine binding site number: 1; 2; 3; 4;

Fluorine binding site 1 out of 4 in 6qhp

Go back to Fluorine Binding Sites List in 6qhp
Fluorine binding site 1 out of 4 in the Time Resolved Structural Analysis of the Full Turnover of An Enzyme - 2256 Ms Covalent Intermediate 1


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 - 2256 Ms Covalent Intermediate 1 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F401

b:13.5
occ:0.08
 F A:FAH401 0.0 13.5 0.1
C2 A:ASB110 1.2 18.4 0.6
CH3 A:FAH401 1.4 17.8 0.1
C1 A:ASB110 2.3 19.4 0.6
C A:FAH401 2.4 19.0 0.1
OD1 A:ASB110 2.4 12.2 0.6
O2 A:ASB110 2.5 19.2 0.6
F A:FAH401 2.5 18.9 0.3
OH A:TYR219 2.5 17.5 1.0
O A:FAH401 2.6 18.9 0.1
OD2 A:ASB110 2.8 5.5 0.6
CG A:ASB110 3.0 8.9 0.6
CH3 A:FAH401 3.1 20.1 0.3
O1 A:ASB110 3.4 22.0 0.6
OXT A:FAH401 3.5 21.1 0.1
CD1 A:PHE40 3.5 11.7 1.0
CH2 A:TRP185 3.5 17.9 1.0
O A:PHE40 3.6 14.4 1.0
CZ3 A:TRP185 3.6 19.6 1.0
O A:FAH401 3.7 10.7 0.3
C A:FAH401 3.8 14.3 0.3
CB A:PHE40 3.8 10.0 1.0
CZ A:TYR219 3.9 10.4 1.0
NE2 A:HIS155 4.0 16.6 1.0
CG A:PHE40 4.1 14.7 1.0
CD A:ARG111 4.3 11.7 1.0
C A:PHE40 4.3 10.7 1.0
O A:HOH546 4.4 16.4 1.0
CD2 A:HIS155 4.4 16.1 1.0
CE1 A:PHE40 4.5 13.1 1.0
CB A:ASB110 4.5 7.7 0.6
CA A:PHE40 4.5 9.2 1.0
CZ2 A:TRP185 4.5 18.7 1.0
N A:PHE40 4.5 8.2 1.0
CE1 A:TYR219 4.6 10.3 1.0
CE3 A:TRP185 4.6 19.7 1.0
NE2 A:HIS280 4.6 13.8 1.0
CE2 A:TYR219 4.7 15.3 1.0
OXT A:FAH401 4.8 13.9 0.3
CG A:ARG111 4.9 9.1 1.0
NH1 A:ARG111 5.0 12.5 1.0

Fluorine binding site 2 out of 4 in 6qhp

Go back to Fluorine Binding Sites List in 6qhp
Fluorine binding site 2 out of 4 in the Time Resolved Structural Analysis of the Full Turnover of An Enzyme - 2256 Ms Covalent Intermediate 1


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 - 2256 Ms Covalent Intermediate 1 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F401

b:18.9
occ:0.31
 F A:FAH401 0.0 18.9 0.3
O2 A:ASB110 0.4 19.2 0.6
O A:FAH401 0.5 18.9 0.1
C A:FAH401 0.8 19.0 0.1
C1 A:ASB110 0.9 19.4 0.6
CH3 A:FAH401 1.3 20.1 0.3
OXT A:FAH401 1.8 21.1 0.1
O1 A:ASB110 1.8 22.0 0.6
CH3 A:FAH401 2.1 17.8 0.1
C2 A:ASB110 2.2 18.4 0.6
C A:FAH401 2.4 14.3 0.3
F A:FAH401 2.5 13.5 0.1
O A:FAH401 2.7 10.7 0.3
NE1 A:TRP156 2.9 15.1 1.0
NE2 A:HIS155 3.0 16.6 1.0
OH A:TYR219 3.0 17.5 1.0
OD1 A:ASB110 3.4 12.2 0.6
OXT A:FAH401 3.5 13.9 0.3
CE2 A:TRP156 3.8 15.0 1.0
CD1 A:TRP156 3.8 15.7 1.0
CE1 A:HIS155 3.9 18.3 1.0
CD2 A:HIS155 3.9 16.1 1.0
CZ A:TYR219 4.1 10.4 1.0
CZ2 A:TRP156 4.1 16.4 1.0
CE2 A:TYR219 4.2 15.3 1.0
NH1 A:ARG111 4.2 12.5 1.0
CG A:ASB110 4.4 8.9 0.6
OD2 A:ASB110 4.6 5.5 0.6
CD1 A:ILE253 4.6 19.6 1.0
CH2 A:TRP185 4.6 17.9 1.0
O A:HOH509 4.7 19.3 1.0
CZ2 A:TRP185 5.0 18.7 1.0

Fluorine binding site 3 out of 4 in 6qhp

Go back to Fluorine Binding Sites List in 6qhp
Fluorine binding site 3 out of 4 in the Time Resolved Structural Analysis of the Full Turnover of An Enzyme - 2256 Ms Covalent Intermediate 1


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Time Resolved Structural Analysis of the Full Turnover of An Enzyme - 2256 Ms Covalent Intermediate 1 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:F401

b:20.4
occ:0.54
 F B:FAH401 0.0 20.4 0.5
CH3 B:FAH401 1.0 25.0 0.5
CH3 B:FAH401 1.6 25.7 0.5
F B:FAH401 2.0 22.3 0.5
C B:FAH401 2.4 19.9 0.5
OXT B:FAH401 2.5 19.9 0.5
C B:FAH401 2.5 20.1 0.5
OH B:TYR219 2.8 19.9 1.0
NE1 B:TRP156 2.8 14.6 1.0
NE2 B:HIS155 3.0 16.9 1.0
OXT B:FAH401 3.0 19.6 0.5
O B:FAH401 3.4 25.5 0.5
O B:FAH401 3.6 23.4 0.5
OD1 B:ASP110 3.6 17.1 1.0
CZ B:TYR219 3.7 17.5 1.0
CD1 B:TRP156 3.8 15.3 1.0
CE2 B:TYR219 3.8 14.9 1.0
NH1 B:ARG111 3.8 16.3 1.0
CE2 B:TRP156 3.8 18.2 1.0
CE1 B:HIS155 3.9 20.1 1.0
CD2 B:HIS155 3.9 19.5 1.0
CZ2 B:TRP156 4.2 19.9 1.0
OD2 B:ASP110 4.2 14.2 1.0
CG B:ASP110 4.3 16.9 1.0
CD B:ARG111 4.6 17.9 1.0
CD1 B:ILE253 4.7 24.9 1.0
CH2 B:TRP185 4.9 30.6 1.0
CZ B:ARG111 5.0 14.2 1.0
CG B:TRP156 5.0 14.8 1.0
CE1 B:TYR219 5.0 15.5 1.0

Fluorine binding site 4 out of 4 in 6qhp

Go back to Fluorine Binding Sites List in 6qhp
Fluorine binding site 4 out of 4 in the Time Resolved Structural Analysis of the Full Turnover of An Enzyme - 2256 Ms Covalent Intermediate 1


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 4 of Time Resolved Structural Analysis of the Full Turnover of An Enzyme - 2256 Ms Covalent Intermediate 1 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:F401

b:22.3
occ:0.46
 F B:FAH401 0.0 22.3 0.5
CH3 B:FAH401 1.0 25.7 0.5
CH3 B:FAH401 1.5 25.0 0.5
F B:FAH401 2.0 20.4 0.5
C B:FAH401 2.4 20.1 0.5
C B:FAH401 2.5 19.9 0.5
O B:FAH401 2.6 25.5 0.5
NE1 B:TRP156 3.1 14.6 1.0
O B:FAH401 3.2 23.4 0.5
OXT B:FAH401 3.3 19.9 0.5
O B:HOH525 3.3 31.2 1.0
OXT B:FAH401 3.5 19.6 0.5
CD1 B:ILE253 3.5 24.9 1.0
CG2 B:ILE253 3.8 25.3 1.0
CE2 B:TRP156 3.9 18.2 1.0
CE2 B:TYR141 3.9 29.4 1.0
NE2 B:HIS155 3.9 16.9 1.0
OD1 B:ASP110 4.0 17.1 1.0
CZ2 B:TRP156 4.0 19.9 1.0
CD1 B:TRP156 4.2 15.3 1.0
NH1 B:ARG114 4.2 17.5 1.0
CE1 B:HIS155 4.3 20.1 1.0
CG2 B:ILE153 4.6 24.8 1.0
CD2 B:TYR141 4.7 25.9 1.0
CB B:ILE253 4.7 36.1 1.0
CG1 B:ILE253 4.7 39.8 1.0
OH B:TYR219 4.7 19.9 1.0
OH B:TYR141 4.8 28.8 1.0
CZ B:TYR141 4.8 34.2 1.0
CG B:ASP110 4.9 16.9 1.0
CE1 B:HIS280 5.0 24.3 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: Fri Aug 2 00:50:50 2024

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