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Fluorine in PDB 4b6s: Structure of Helicobacter Pylori Type II Dehydroquinase Inhibited By (2S)-2-Perfluorobenzyl-3-Dehydroquinic Acid

Enzymatic activity of Structure of Helicobacter Pylori Type II Dehydroquinase Inhibited By (2S)-2-Perfluorobenzyl-3-Dehydroquinic Acid

All present enzymatic activity of Structure of Helicobacter Pylori Type II Dehydroquinase Inhibited By (2S)-2-Perfluorobenzyl-3-Dehydroquinic Acid:
4.2.1.10;

Protein crystallography data

The structure of Structure of Helicobacter Pylori Type II Dehydroquinase Inhibited By (2S)-2-Perfluorobenzyl-3-Dehydroquinic Acid, PDB code: 4b6s was solved by J.M.Otero, A.L.Llamas-Saiz, E.Lence, L.Tizon, A.Peon, V.F.V.Prazeres, H.Lamb, A.R.Hawkins, C.Gonzalez-Bello, M.J.Van Raaij, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 58.65 / 1.90
Space group P 42 2 2
Cell size a, b, c (Å), α, β, γ (°) 100.190, 100.190, 104.580, 90.00, 90.00, 90.00
R / Rfree (%) 22.6 / 27.8

Fluorine Binding Sites:

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 15;

Binding sites:

The binding sites of Fluorine atom in the Structure of Helicobacter Pylori Type II Dehydroquinase Inhibited By (2S)-2-Perfluorobenzyl-3-Dehydroquinic Acid (pdb code 4b6s). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 15 binding sites of Fluorine where determined in the Structure of Helicobacter Pylori Type II Dehydroquinase Inhibited By (2S)-2-Perfluorobenzyl-3-Dehydroquinic Acid, PDB code: 4b6s:
Jump to Fluorine binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Fluorine binding site 1 out of 15 in 4b6s

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Fluorine binding site 1 out of 15 in the Structure of Helicobacter Pylori Type II Dehydroquinase Inhibited By (2S)-2-Perfluorobenzyl-3-Dehydroquinic Acid


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Structure of Helicobacter Pylori Type II Dehydroquinase Inhibited By (2S)-2-Perfluorobenzyl-3-Dehydroquinic Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F200

b:33.5
occ:1.00
 FAK A:2HN200 0.0 33.5 1.0
CAT A:2HN200 1.3 31.6 1.0
CAR A:2HN200 2.3 30.9 1.0
CAU A:2HN200 2.4 30.2 1.0
FAI A:2HN200 2.7 30.2 1.0
CAL A:2HN200 2.9 26.0 1.0
CD1 A:LEU103 3.2 24.8 1.0
CD1 A:LEU11 3.4 24.5 1.0
CAX A:2HN200 3.6 23.1 1.0
CAP A:2HN200 3.6 32.7 1.0
CAS A:2HN200 3.6 31.7 1.0
OAC A:2HN200 4.0 20.4 1.0
CD1 A:TYR22 4.0 57.4 1.0
CD2 A:LEU14 4.0 28.9 1.0
CAQ A:2HN200 4.1 32.9 1.0
CG A:LEU103 4.2 22.2 1.0
CE1 A:TYR22 4.2 56.3 1.0
CG A:TYR22 4.2 59.0 1.0
CAN A:2HN200 4.2 18.1 1.0
CD2 A:LEU11 4.3 24.0 1.0
CG A:LEU14 4.4 29.9 1.0
CG A:LEU11 4.5 21.4 1.0
CZ A:TYR22 4.6 55.4 1.0
CD2 A:TYR22 4.6 58.5 1.0
CAY A:2HN200 4.6 20.8 1.0
CB A:LEU103 4.6 21.7 1.0
CAO A:2HN200 4.6 22.7 1.0
FAG A:2HN200 4.7 31.0 1.0
OAA A:2HN200 4.7 20.8 1.0
CE2 A:TYR22 4.7 57.3 1.0
FAJ A:2HN200 4.8 34.8 1.0
CD1 A:LEU14 4.8 27.4 1.0
OAB A:2HN200 4.8 27.4 1.0
CB A:TYR22 4.8 60.1 1.0
CA A:LEU11 4.9 22.4 1.0

Fluorine binding site 2 out of 15 in 4b6s

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Fluorine binding site 2 out of 15 in the Structure of Helicobacter Pylori Type II Dehydroquinase Inhibited By (2S)-2-Perfluorobenzyl-3-Dehydroquinic Acid


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Structure of Helicobacter Pylori Type II Dehydroquinase Inhibited By (2S)-2-Perfluorobenzyl-3-Dehydroquinic Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F200

b:30.2
occ:1.00
 FAI A:2HN200 0.0 30.2 1.0
CAR A:2HN200 1.3 30.9 1.0
CAP A:2HN200 2.3 32.7 1.0
CAT A:2HN200 2.4 31.6 1.0
FAG A:2HN200 2.7 31.0 1.0
FAK A:2HN200 2.7 33.5 1.0
CG A:LEU14 3.2 29.9 1.0
O A:ASN10 3.3 24.1 1.0
CD2 A:LEU14 3.3 28.9 1.0
CAQ A:2HN200 3.6 32.9 1.0
CAU A:2HN200 3.6 30.2 1.0
N A:LEU14 3.8 28.2 1.0
CA A:LEU11 3.9 22.4 1.0
CA A:LEU14 4.0 31.2 1.0
CAS A:2HN200 4.0 31.7 1.0
C A:ASN10 4.1 21.8 1.0
CB A:LEU14 4.2 29.9 1.0
O A:LEU11 4.2 23.4 1.0
CD1 A:LEU14 4.3 27.4 1.0
CD2 A:TYR22 4.3 58.5 1.0
CD1 A:LEU11 4.3 24.5 1.0
C A:LEU11 4.4 23.7 1.0
C A:MET13 4.4 26.6 1.0
N A:LEU11 4.4 22.4 1.0
O A:HOH2013 4.4 53.3 1.0
CG A:TYR22 4.5 59.0 1.0
FAH A:2HN200 4.6 36.9 1.0
CE2 A:TYR22 4.7 57.3 1.0
N A:MET13 4.8 24.6 1.0
CD1 A:LEU103 4.9 24.8 1.0
CB A:TYR22 4.9 60.1 1.0
CAL A:2HN200 4.9 26.0 1.0
O A:MET13 4.9 27.6 1.0
CA A:MET13 5.0 25.3 1.0
O A:HOH2012 5.0 25.6 1.0
CB A:LEU11 5.0 23.4 1.0

Fluorine binding site 3 out of 15 in 4b6s

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Fluorine binding site 3 out of 15 in the Structure of Helicobacter Pylori Type II Dehydroquinase Inhibited By (2S)-2-Perfluorobenzyl-3-Dehydroquinic Acid


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Structure of Helicobacter Pylori Type II Dehydroquinase Inhibited By (2S)-2-Perfluorobenzyl-3-Dehydroquinic Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F200

b:31.0
occ:1.00
 FAG A:2HN200 0.0 31.0 1.0
CAP A:2HN200 1.3 32.7 1.0
CAQ A:2HN200 2.3 32.9 1.0
CAR A:2HN200 2.4 30.9 1.0
FAH A:2HN200 2.7 36.9 1.0
FAI A:2HN200 2.7 30.2 1.0
O A:ASN10 3.0 24.1 1.0
CD2 C:LEU93 3.1 25.8 1.0
O A:HOH2013 3.3 53.3 1.0
CAS A:2HN200 3.6 31.7 1.0
CAT A:2HN200 3.6 31.6 1.0
CB A:ASN10 3.7 21.2 1.0
C A:ASN10 3.8 21.8 1.0
CB A:MET13 3.9 25.2 1.0
CAU A:2HN200 4.1 30.2 1.0
CA A:ASN10 4.3 20.9 1.0
CE2 A:TYR22 4.4 57.3 1.0
C A:MET13 4.5 26.6 1.0
CA A:MET13 4.6 25.3 1.0
CD2 A:TYR22 4.6 58.5 1.0
CG C:LEU93 4.6 26.8 1.0
FAJ A:2HN200 4.6 34.8 1.0
N A:LEU14 4.7 28.2 1.0
O C:HOH2033 4.7 25.7 1.0
FAK A:2HN200 4.7 33.5 1.0
O A:MET13 4.7 27.6 1.0
CG A:ASN10 4.7 20.9 1.0
CG A:MET13 4.7 24.6 1.0
N A:LEU11 4.8 22.4 1.0
N A:MET13 4.9 24.6 1.0

Fluorine binding site 4 out of 15 in 4b6s

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Fluorine binding site 4 out of 15 in the Structure of Helicobacter Pylori Type II Dehydroquinase Inhibited By (2S)-2-Perfluorobenzyl-3-Dehydroquinic Acid


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 4 of Structure of Helicobacter Pylori Type II Dehydroquinase Inhibited By (2S)-2-Perfluorobenzyl-3-Dehydroquinic Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F200

b:36.9
occ:1.00
 FAH A:2HN200 0.0 36.9 1.0
CAQ A:2HN200 1.3 32.9 1.0
CAP A:2HN200 2.3 32.7 1.0
CAS A:2HN200 2.4 31.7 1.0
FAJ A:2HN200 2.7 34.8 1.0
FAG A:2HN200 2.7 31.0 1.0
O C:HOH2033 3.0 25.7 1.0
CAR A:2HN200 3.6 30.9 1.0
CB C:ASP89 3.6 17.9 1.0
O A:HOH2017 3.6 33.3 1.0
CD2 C:LEU93 3.6 25.8 1.0
CAU A:2HN200 3.7 30.2 1.0
CB A:ASN10 3.7 21.2 1.0
CG C:ASP89 4.1 23.1 1.0
O C:ASP89 4.1 20.8 1.0
CAT A:2HN200 4.1 31.6 1.0
CE2 A:TYR22 4.2 57.3 1.0
OH A:TYR22 4.2 51.2 1.0
OD2 C:ASP89 4.3 25.4 1.0
CG A:ASN10 4.3 20.9 1.0
C C:ASP89 4.3 20.3 1.0
ND2 A:ASN10 4.4 19.9 1.0
CA C:ASP89 4.4 19.6 1.0
CZ A:TYR22 4.5 55.4 1.0
FAI A:2HN200 4.6 30.2 1.0
O A:HOH2013 4.7 53.3 1.0
OD1 C:ASP89 4.7 25.2 1.0
CG C:LEU93 4.7 26.8 1.0
O A:HOH2005 4.9 24.6 1.0
OAB A:2HN200 4.9 27.4 1.0
O A:ASN10 4.9 24.1 1.0
CAL A:2HN200 5.0 26.0 1.0

Fluorine binding site 5 out of 15 in 4b6s

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Fluorine binding site 5 out of 15 in the Structure of Helicobacter Pylori Type II Dehydroquinase Inhibited By (2S)-2-Perfluorobenzyl-3-Dehydroquinic Acid


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 5 of Structure of Helicobacter Pylori Type II Dehydroquinase Inhibited By (2S)-2-Perfluorobenzyl-3-Dehydroquinic Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F200

b:34.8
occ:1.00
 FAJ A:2HN200 0.0 34.8 1.0
CAS A:2HN200 1.3 31.7 1.0
CAQ A:2HN200 2.3 32.9 1.0
CAU A:2HN200 2.4 30.2 1.0
FAH A:2HN200 2.7 36.9 1.0
OH A:TYR22 2.9 51.2 1.0
CAL A:2HN200 3.0 26.0 1.0
CAO A:2HN200 3.1 22.7 1.0
OD2 C:ASP89 3.1 25.4 1.0
OAB A:2HN200 3.2 27.4 1.0
CAW A:2HN200 3.2 19.6 1.0
O A:HOH2017 3.3 33.3 1.0
CG C:ASP89 3.5 23.1 1.0
OAE A:2HN200 3.5 24.5 1.0
CAP A:2HN200 3.6 32.7 1.0
CZ A:TYR22 3.6 55.4 1.0
CAT A:2HN200 3.6 31.6 1.0
CAX A:2HN200 3.6 23.1 1.0
OD1 C:ASP89 3.9 25.2 1.0
CAR A:2HN200 4.0 30.9 1.0
CB C:ASP89 4.1 17.9 1.0
CE2 A:TYR22 4.2 57.3 1.0
CE1 A:TYR22 4.4 56.3 1.0
NH1 A:ARG113 4.4 21.4 1.0
O A:HOH2005 4.4 24.6 1.0
O C:HOH2033 4.6 25.7 1.0
FAG A:2HN200 4.6 31.0 1.0
CAV A:2HN200 4.7 20.8 1.0
FAK A:2HN200 4.8 33.5 1.0
CAY A:2HN200 4.9 20.8 1.0
CAM A:2HN200 4.9 21.4 1.0
CZ A:ARG113 5.0 27.0 1.0
NH2 A:ARG113 5.0 27.9 1.0

Fluorine binding site 6 out of 15 in 4b6s

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Fluorine binding site 6 out of 15 in the Structure of Helicobacter Pylori Type II Dehydroquinase Inhibited By (2S)-2-Perfluorobenzyl-3-Dehydroquinic Acid


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 6 of Structure of Helicobacter Pylori Type II Dehydroquinase Inhibited By (2S)-2-Perfluorobenzyl-3-Dehydroquinic Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
B:F200

b:28.4
occ:1.00
 FAK B:2HN200 0.0 28.4 1.0
CAT B:2HN200 1.3 29.1 1.0
CAR B:2HN200 2.3 28.1 1.0
CAU B:2HN200 2.4 27.8 1.0
FAI B:2HN200 2.8 29.3 1.0
CAL B:2HN200 2.8 24.9 1.0
CD1 B:LEU103 3.4 26.1 1.0
CD1 B:LEU11 3.4 23.3 1.0
CAX B:2HN200 3.5 24.6 1.0
CAP B:2HN200 3.6 28.7 1.0
CAS B:2HN200 3.6 28.9 1.0
CD2 B:LEU14 3.8 26.5 1.0
CD1 B:TYR22 4.0 61.0 1.0
CAQ B:2HN200 4.1 29.5 1.0
OAC B:2HN200 4.1 20.8 1.0
CE1 B:TYR22 4.2 59.5 1.0
CG B:LEU103 4.3 21.6 1.0
CAN B:2HN200 4.3 19.0 1.0
CG B:LEU14 4.3 27.2 1.0
CG B:TYR22 4.3 62.5 1.0
CAY B:2HN200 4.6 22.6 1.0
CG B:LEU11 4.6 23.1 1.0
CD2 B:LEU11 4.6 23.0 1.0
CAO B:2HN200 4.6 24.4 1.0
CZ B:TYR22 4.6 58.2 1.0
FAG B:2HN200 4.7 30.3 1.0
CB B:LEU103 4.7 21.6 1.0
OAA B:2HN200 4.7 21.3 1.0
CD2 B:TYR22 4.7 61.0 1.0
FAJ B:2HN200 4.8 30.8 1.0
OAB B:2HN200 4.8 26.9 1.0
CB B:TYR22 4.8 63.4 1.0
CD1 B:LEU14 4.8 26.4 1.0
CA B:LEU11 4.9 21.1 1.0
CE2 B:TYR22 4.9 59.9 1.0

Fluorine binding site 7 out of 15 in 4b6s

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Fluorine binding site 7 out of 15 in the Structure of Helicobacter Pylori Type II Dehydroquinase Inhibited By (2S)-2-Perfluorobenzyl-3-Dehydroquinic Acid


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 7 of Structure of Helicobacter Pylori Type II Dehydroquinase Inhibited By (2S)-2-Perfluorobenzyl-3-Dehydroquinic Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
B:F200

b:29.3
occ:1.00
 FAI B:2HN200 0.0 29.3 1.0
CAR B:2HN200 1.3 28.1 1.0
CAP B:2HN200 2.3 28.7 1.0
CAT B:2HN200 2.4 29.1 1.0
FAG B:2HN200 2.6 30.3 1.0
FAK B:2HN200 2.8 28.4 1.0
O B:ASN10 3.1 21.2 1.0
CD2 B:LEU14 3.1 26.5 1.0
CG B:LEU14 3.2 27.2 1.0
CAQ B:2HN200 3.6 29.5 1.0
N B:LEU14 3.6 26.4 1.0
CAU B:2HN200 3.7 27.8 1.0
CA B:LEU14 3.8 28.8 1.0
CA B:LEU11 3.9 21.1 1.0
O B:HOH2007 4.0 47.2 1.0
C B:ASN10 4.0 19.6 1.0
CB B:LEU14 4.0 27.7 1.0
CAS B:2HN200 4.1 28.9 1.0
O B:LEU11 4.2 19.7 1.0
C B:MET13 4.2 24.5 1.0
C B:LEU11 4.4 20.8 1.0
CD1 B:LEU11 4.4 23.3 1.0
N B:LEU11 4.4 20.3 1.0
CD1 B:LEU14 4.5 26.4 1.0
FAH B:2HN200 4.6 31.2 1.0
CD2 B:TYR22 4.6 61.0 1.0
CG B:TYR22 4.7 62.5 1.0
O B:MET13 4.8 25.2 1.0
N B:MET13 4.8 22.3 1.0
CA B:MET13 4.9 23.3 1.0
CB B:TYR22 4.9 63.4 1.0
CB B:MET13 4.9 22.2 1.0
CAL B:2HN200 5.0 24.9 1.0
O B:HOH2006 5.0 26.1 1.0

Fluorine binding site 8 out of 15 in 4b6s

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Fluorine binding site 8 out of 15 in the Structure of Helicobacter Pylori Type II Dehydroquinase Inhibited By (2S)-2-Perfluorobenzyl-3-Dehydroquinic Acid


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 8 of Structure of Helicobacter Pylori Type II Dehydroquinase Inhibited By (2S)-2-Perfluorobenzyl-3-Dehydroquinic Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
B:F200

b:30.3
occ:1.00
 FAG B:2HN200 0.0 30.3 1.0
CAP B:2HN200 1.3 28.7 1.0
CAR B:2HN200 2.3 28.1 1.0
CAQ B:2HN200 2.3 29.5 1.0
FAI B:2HN200 2.6 29.3 1.0
FAH B:2HN200 2.7 31.2 1.0
O B:ASN10 2.8 21.2 1.0
CD2 A:LEU93 3.2 27.5 1.0
O B:HOH2007 3.4 47.2 1.0
CAT B:2HN200 3.6 29.1 1.0
CAS B:2HN200 3.6 28.9 1.0
CB B:ASN10 3.6 17.9 1.0
C B:ASN10 3.7 19.6 1.0
CB B:MET13 3.8 22.2 1.0
CAU B:2HN200 4.1 27.8 1.0
CA B:ASN10 4.2 18.3 1.0
C B:MET13 4.4 24.5 1.0
CG B:MET13 4.5 24.0 1.0
CA B:MET13 4.6 23.3 1.0
N B:LEU14 4.6 26.4 1.0
FAJ B:2HN200 4.6 30.8 1.0
O A:HOH2063 4.6 27.0 1.0
FAK B:2HN200 4.7 28.4 1.0
O B:MET13 4.7 25.2 1.0
CG A:LEU93 4.7 24.0 1.0
CG B:ASN10 4.7 20.5 1.0
N B:LEU11 4.8 20.3 1.0
CD2 B:TYR22 4.8 61.0 1.0
CE2 B:TYR22 4.8 59.9 1.0
N B:MET13 4.9 22.3 1.0

Fluorine binding site 9 out of 15 in 4b6s

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Fluorine binding site 9 out of 15 in the Structure of Helicobacter Pylori Type II Dehydroquinase Inhibited By (2S)-2-Perfluorobenzyl-3-Dehydroquinic Acid


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 9 of Structure of Helicobacter Pylori Type II Dehydroquinase Inhibited By (2S)-2-Perfluorobenzyl-3-Dehydroquinic Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
B:F200

b:31.2
occ:1.00
 FAH B:2HN200 0.0 31.2 1.0
CAQ B:2HN200 1.3 29.5 1.0
CAP B:2HN200 2.3 28.7 1.0
CAS B:2HN200 2.4 28.9 1.0
FAJ B:2HN200 2.6 30.8 1.0
FAG B:2HN200 2.7 30.3 1.0
O A:HOH2063 2.9 27.0 1.0
CAR B:2HN200 3.6 28.1 1.0
CB B:ASN10 3.6 17.9 1.0
CB A:ASP89 3.6 17.6 1.0
CAU B:2HN200 3.7 27.8 1.0
CD2 A:LEU93 3.7 27.5 1.0
O A:HOH2064 3.8 37.5 1.0
CAT B:2HN200 4.1 29.1 1.0
O A:ASP89 4.1 18.4 1.0
CG A:ASP89 4.1 22.4 1.0
CG B:ASN10 4.2 20.5 1.0
CE2 B:TYR22 4.3 59.9 1.0
ND2 B:ASN10 4.3 20.6 1.0
C A:ASP89 4.3 17.8 1.0
CA A:ASP89 4.4 18.5 1.0
OD2 A:ASP89 4.4 26.4 1.0
O B:ASN10 4.6 21.2 1.0
FAI B:2HN200 4.6 29.3 1.0
OH B:TYR22 4.6 55.1 1.0
O A:HOH2066 4.7 21.4 1.0
CZ B:TYR22 4.7 58.2 1.0
OD1 A:ASP89 4.8 23.3 1.0
CG A:LEU93 4.8 24.0 1.0
OAB B:2HN200 4.8 26.9 1.0
O B:HOH2007 4.8 47.2 1.0
CA B:ASN10 4.9 18.3 1.0
OD1 B:ASN10 5.0 21.2 1.0
CAL B:2HN200 5.0 24.9 1.0

Fluorine binding site 10 out of 15 in 4b6s

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Fluorine binding site 10 out of 15 in the Structure of Helicobacter Pylori Type II Dehydroquinase Inhibited By (2S)-2-Perfluorobenzyl-3-Dehydroquinic Acid


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 10 of Structure of Helicobacter Pylori Type II Dehydroquinase Inhibited By (2S)-2-Perfluorobenzyl-3-Dehydroquinic Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
B:F200

b:30.8
occ:1.00
 FAJ B:2HN200 0.0 30.8 1.0
CAS B:2HN200 1.3 28.9 1.0
CAQ B:2HN200 2.3 29.5 1.0
CAU B:2HN200 2.4 27.8 1.0
FAH B:2HN200 2.6 31.2 1.0
OH B:TYR22 3.0 55.1 1.0
CAL B:2HN200 3.0 24.9 1.0
CAO B:2HN200 3.1 24.4 1.0
OAB B:2HN200 3.2 26.9 1.0
O A:HOH2064 3.2 37.5 1.0
OD2 A:ASP89 3.2 26.4 1.0
CAW B:2HN200 3.3 25.4 1.0
CG A:ASP89 3.5 22.4 1.0
CAP B:2HN200 3.6 28.7 1.0
CZ B:TYR22 3.6 58.2 1.0
CAT B:2HN200 3.6 29.1 1.0
CAX B:2HN200 3.7 24.6 1.0
OAE B:2HN200 3.7 27.0 1.0
OD1 A:ASP89 3.9 23.3 1.0
CB A:ASP89 4.0 17.6 1.0
CE2 B:TYR22 4.1 59.9 1.0
CAR B:2HN200 4.1 28.1 1.0
O A:HOH2063 4.3 27.0 1.0
O A:HOH2066 4.3 21.4 1.0
NH1 B:ARG113 4.4 21.2 1.0
CE1 B:TYR22 4.5 59.5 1.0
FAG B:2HN200 4.6 30.3 1.0
CAV B:2HN200 4.7 25.2 1.0
FAK B:2HN200 4.8 28.4 1.0
CAY B:2HN200 4.9 22.6 1.0
NH1 B:ARG109 4.9 30.4 1.0
CAM B:2HN200 5.0 24.6 1.0

Reference:

E.Lence, L.Tizon, J.M.Otero, A.Peon, V.F.Prazeres, A.L.Llamas-Saiz, G.C.Fox, M.J.Van Raaij, H.Lamb, A.R.Hawkins, C.Gonzalez-Bello. Mechanistic Basis of the Inhibition of Type II Dehydroquinase By (2S)- and (2R)-2-Benzyl-3-Dehydroquinic Acids. Acs Chem. Biol. V. 8 568 2013.
ISSN: ESSN 1554-8937
PubMed: 23198883
DOI: 10.1021/CB300493S
Page generated: Mon Jul 14 20:30:41 2025

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