Atomistry » Fluorine » PDB 6q0t-6qhv » 6qhp
Atomistry »
  Fluorine »
    PDB 6q0t-6qhv »
      6qhp »

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

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy