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Fluorine in PDB 7jx9: The Crystal Structure of Human Ornithine Aminotransferase with An Intermediate Bound During Inactivation By (1S,3S)-3-Amino-4- (Hexafluoropropan-2-Ylidenyl)-Cyclopentane-1-Carboxylic Acid.

Enzymatic activity of The Crystal Structure of Human Ornithine Aminotransferase with An Intermediate Bound During Inactivation By (1S,3S)-3-Amino-4- (Hexafluoropropan-2-Ylidenyl)-Cyclopentane-1-Carboxylic Acid.

All present enzymatic activity of The Crystal Structure of Human Ornithine Aminotransferase with An Intermediate Bound During Inactivation By (1S,3S)-3-Amino-4- (Hexafluoropropan-2-Ylidenyl)-Cyclopentane-1-Carboxylic Acid.:
2.6.1.13;

Protein crystallography data

The structure of The Crystal Structure of Human Ornithine Aminotransferase with An Intermediate Bound During Inactivation By (1S,3S)-3-Amino-4- (Hexafluoropropan-2-Ylidenyl)-Cyclopentane-1-Carboxylic Acid., PDB code: 7jx9 was solved by A.Butrin, B.Beaupre, S.Shen, R.B.Silverman, G.Moran, D.Liu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.21 / 1.96
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 115.304, 115.304, 185.431, 90, 90, 120
R / Rfree (%) 18.6 / 21.3

Fluorine Binding Sites:

Pages:

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

Binding sites:

The binding sites of Fluorine atom in the The Crystal Structure of Human Ornithine Aminotransferase with An Intermediate Bound During Inactivation By (1S,3S)-3-Amino-4- (Hexafluoropropan-2-Ylidenyl)-Cyclopentane-1-Carboxylic Acid. (pdb code 7jx9). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 15 binding sites of Fluorine where determined in the The Crystal Structure of Human Ornithine Aminotransferase with An Intermediate Bound During Inactivation By (1S,3S)-3-Amino-4- (Hexafluoropropan-2-Ylidenyl)-Cyclopentane-1-Carboxylic Acid., PDB code: 7jx9:
Jump to Fluorine binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Fluorine binding site 1 out of 15 in 7jx9

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Fluorine binding site 1 out of 15 in the The Crystal Structure of Human Ornithine Aminotransferase with An Intermediate Bound During Inactivation By (1S,3S)-3-Amino-4- (Hexafluoropropan-2-Ylidenyl)-Cyclopentane-1-Carboxylic Acid.


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of The Crystal Structure of Human Ornithine Aminotransferase with An Intermediate Bound During Inactivation By (1S,3S)-3-Amino-4- (Hexafluoropropan-2-Ylidenyl)-Cyclopentane-1-Carboxylic Acid. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F501

b:68.9
occ:1.00
 F28 A:IF1501 0.0 68.9 1.0
C02 A:IF1501 1.4 69.5 1.0
F30 A:IF1501 2.3 64.5 1.0
F29 A:IF1501 2.3 73.7 1.0
C25 A:IF1501 2.5 54.8 1.0
C23 A:IF1501 3.0 45.3 1.0
CE1 A:TYR85 3.0 44.2 1.0
C24 A:IF1501 3.2 45.2 1.0
C03 A:IF1501 3.4 59.1 1.0
CD1 A:TYR85 3.5 44.6 1.0
CZ A:TYR85 3.5 45.0 1.0
F32 A:IF1501 3.6 59.6 1.0
OH A:TYR85 3.9 48.0 1.0
CG A:GLU235 4.0 57.8 1.0
CG A:TYR85 4.3 43.2 1.0
CE2 A:TYR85 4.4 44.1 1.0
C20 A:IF1501 4.4 44.6 1.0
OE1 A:GLU235 4.4 69.8 1.0
C22 A:IF1501 4.6 41.9 1.0
F31 A:IF1501 4.7 56.8 1.0
CD2 A:TYR85 4.7 41.9 1.0
CD A:GLU235 4.8 65.1 1.0
O26 A:IF1501 4.9 42.1 1.0
CB A:GLU235 5.0 49.7 1.0
C01 A:IF1501 5.0 45.3 1.0
NH1 A:ARG413 5.0 60.2 1.0

Fluorine binding site 2 out of 15 in 7jx9

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Fluorine binding site 2 out of 15 in the The Crystal Structure of Human Ornithine Aminotransferase with An Intermediate Bound During Inactivation By (1S,3S)-3-Amino-4- (Hexafluoropropan-2-Ylidenyl)-Cyclopentane-1-Carboxylic Acid.


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of The Crystal Structure of Human Ornithine Aminotransferase with An Intermediate Bound During Inactivation By (1S,3S)-3-Amino-4- (Hexafluoropropan-2-Ylidenyl)-Cyclopentane-1-Carboxylic Acid. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F501

b:73.7
occ:1.00
 F29 A:IF1501 0.0 73.7 1.0
C02 A:IF1501 1.4 69.5 1.0
C25 A:IF1501 2.3 54.8 1.0
F28 A:IF1501 2.3 68.9 1.0
F30 A:IF1501 2.3 64.5 1.0
C24 A:IF1501 2.8 45.2 1.0
CG A:GLU235 2.8 57.8 1.0
C23 A:IF1501 3.1 45.3 1.0
C20 A:IF1501 3.3 44.6 1.0
C03 A:IF1501 3.3 59.1 1.0
F32 A:IF1501 3.7 59.6 1.0
CB A:GLU235 3.7 49.7 1.0
N19 A:IF1501 3.8 38.8 1.0
CD A:GLU235 3.9 65.1 1.0
C21 A:IF1501 4.0 41.8 1.0
CE1 A:PHE177 4.0 37.7 1.0
OE1 A:GLU235 4.0 69.8 1.0
CD1 A:PHE177 4.1 32.6 1.0
C22 A:IF1501 4.3 41.9 1.0
O26 A:IF1501 4.3 42.1 1.0
CZ A:PHE177 4.4 33.8 1.0
F31 A:IF1501 4.5 56.8 1.0
CG A:PHE177 4.6 35.6 1.0
CA A:GLU235 4.6 47.0 1.0
C01 A:IF1501 4.7 45.3 1.0
CE2 A:PHE177 4.9 37.5 1.0
OE2 A:GLU235 4.9 68.2 1.0
CD2 A:PHE177 4.9 35.7 1.0
C18 A:IF1501 5.0 39.0 1.0

Fluorine binding site 3 out of 15 in 7jx9

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Fluorine binding site 3 out of 15 in the The Crystal Structure of Human Ornithine Aminotransferase with An Intermediate Bound During Inactivation By (1S,3S)-3-Amino-4- (Hexafluoropropan-2-Ylidenyl)-Cyclopentane-1-Carboxylic Acid.


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of The Crystal Structure of Human Ornithine Aminotransferase with An Intermediate Bound During Inactivation By (1S,3S)-3-Amino-4- (Hexafluoropropan-2-Ylidenyl)-Cyclopentane-1-Carboxylic Acid. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F501

b:64.5
occ:1.00
 F30 A:IF1501 0.0 64.5 1.0
C02 A:IF1501 1.4 69.5 1.0
F32 A:IF1501 2.0 59.6 1.0
F28 A:IF1501 2.3 68.9 1.0
C25 A:IF1501 2.3 54.8 1.0
F29 A:IF1501 2.3 73.7 1.0
C03 A:IF1501 2.6 59.1 1.0
CG A:GLU235 2.9 57.8 1.0
CB A:GLU235 3.2 49.7 1.0
CA A:GLU235 3.3 47.0 1.0
NH1 A:ARG413 3.5 60.2 1.0
C24 A:IF1501 3.7 45.2 1.0
N A:GLU235 3.8 42.9 1.0
NH2 A:ARG413 3.9 59.0 1.0
F31 A:IF1501 3.9 56.8 1.0
CZ A:ARG413 4.1 61.9 1.0
CD A:GLU235 4.2 65.1 1.0
C23 A:IF1501 4.3 45.3 1.0
OE1 A:GLU235 4.4 69.8 1.0
C A:GLY234 4.4 44.6 1.0
CD1 A:TYR85 4.5 44.6 1.0
CE1 A:TYR85 4.5 44.2 1.0
OE1 A:GLN266 4.6 58.0 1.0
O A:HOH722 4.6 39.4 1.0
C20 A:IF1501 4.6 44.6 1.0
C A:GLU235 4.6 39.3 1.0
O A:GLY234 4.7 40.8 1.0
N19 A:IF1501 4.7 38.8 1.0
O A:GLU235 4.9 44.1 1.0

Fluorine binding site 4 out of 15 in 7jx9

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Fluorine binding site 4 out of 15 in the The Crystal Structure of Human Ornithine Aminotransferase with An Intermediate Bound During Inactivation By (1S,3S)-3-Amino-4- (Hexafluoropropan-2-Ylidenyl)-Cyclopentane-1-Carboxylic Acid.


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 4 of The Crystal Structure of Human Ornithine Aminotransferase with An Intermediate Bound During Inactivation By (1S,3S)-3-Amino-4- (Hexafluoropropan-2-Ylidenyl)-Cyclopentane-1-Carboxylic Acid. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F501

b:56.8
occ:1.00
 F31 A:IF1501 0.0 56.8 1.0
C03 A:IF1501 1.4 59.1 1.0
C25 A:IF1501 2.4 54.8 1.0
F32 A:IF1501 2.4 59.6 1.0
NZ A:LYS292 2.4 42.3 1.0
OE1 A:GLN266 2.9 58.0 1.0
C24 A:IF1501 2.9 45.2 1.0
N19 A:IF1501 3.1 38.8 1.0
CE A:LYS292 3.2 39.6 1.0
O10 A:IF1501 3.2 32.3 1.0
C20 A:IF1501 3.3 44.6 1.0
CB A:TYR85 3.4 42.3 1.0
O A:TYR85 3.7 46.5 1.0
CD A:GLN266 3.7 53.8 1.0
C02 A:IF1501 3.8 69.5 1.0
C18 A:IF1501 3.9 39.0 1.0
F30 A:IF1501 3.9 64.5 1.0
CG A:TYR85 4.0 43.2 1.0
CD1 A:TYR85 4.1 44.6 1.0
C23 A:IF1501 4.1 45.3 1.0
CD A:LYS292 4.2 40.0 1.0
CB A:GLN266 4.3 38.0 1.0
C04 A:IF1501 4.3 33.2 1.0
NE2 A:GLN266 4.3 57.5 1.0
CA A:TYR85 4.3 41.3 1.0
C A:TYR85 4.4 40.5 1.0
NH2 A:ARG413 4.5 59.0 1.0
F29 A:IF1501 4.5 73.7 1.0
CG A:GLN266 4.6 47.6 1.0
C09 A:IF1501 4.6 33.5 1.0
F28 A:IF1501 4.7 68.9 1.0
C21 A:IF1501 4.7 41.8 1.0
O A:HOH722 4.8 39.4 1.0

Fluorine binding site 5 out of 15 in 7jx9

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Fluorine binding site 5 out of 15 in the The Crystal Structure of Human Ornithine Aminotransferase with An Intermediate Bound During Inactivation By (1S,3S)-3-Amino-4- (Hexafluoropropan-2-Ylidenyl)-Cyclopentane-1-Carboxylic Acid.


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 5 of The Crystal Structure of Human Ornithine Aminotransferase with An Intermediate Bound During Inactivation By (1S,3S)-3-Amino-4- (Hexafluoropropan-2-Ylidenyl)-Cyclopentane-1-Carboxylic Acid. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F501

b:59.6
occ:1.00
 F32 A:IF1501 0.0 59.6 1.0
C03 A:IF1501 1.4 59.1 1.0
F30 A:IF1501 2.0 64.5 1.0
C25 A:IF1501 2.3 54.8 1.0
F31 A:IF1501 2.4 56.8 1.0
OE1 A:GLN266 2.6 58.0 1.0
C02 A:IF1501 2.7 69.5 1.0
NH2 A:ARG413 2.9 59.0 1.0
NH1 A:ARG413 3.5 60.2 1.0
CZ A:ARG413 3.6 61.9 1.0
CD A:GLN266 3.6 53.8 1.0
F28 A:IF1501 3.6 68.9 1.0
F29 A:IF1501 3.7 73.7 1.0
C24 A:IF1501 3.7 45.2 1.0
O A:HOH722 3.9 39.4 1.0
O10 A:IF1501 4.0 32.3 1.0
NE2 A:GLN266 4.0 57.5 1.0
N A:GLU235 4.1 42.9 1.0
CD1 A:TYR85 4.2 44.6 1.0
CA A:GLU235 4.3 47.0 1.0
N19 A:IF1501 4.3 38.8 1.0
C A:GLY234 4.3 44.6 1.0
CB A:GLU235 4.5 49.7 1.0
C20 A:IF1501 4.5 44.6 1.0
CA A:GLY234 4.6 36.8 1.0
CG A:GLU235 4.6 57.8 1.0
C23 A:IF1501 4.7 45.3 1.0
NZ A:LYS292 4.8 42.3 1.0
CB A:TYR85 4.8 42.3 1.0
CG A:TYR85 4.8 43.2 1.0
CE1 A:TYR85 4.8 44.2 1.0
O A:GLY234 4.9 40.8 1.0
NE A:ARG413 4.9 56.2 1.0
CG A:GLN266 4.9 47.6 1.0

Fluorine binding site 6 out of 15 in 7jx9

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Fluorine binding site 6 out of 15 in the The Crystal Structure of Human Ornithine Aminotransferase with An Intermediate Bound During Inactivation By (1S,3S)-3-Amino-4- (Hexafluoropropan-2-Ylidenyl)-Cyclopentane-1-Carboxylic Acid.


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 6 of The Crystal Structure of Human Ornithine Aminotransferase with An Intermediate Bound During Inactivation By (1S,3S)-3-Amino-4- (Hexafluoropropan-2-Ylidenyl)-Cyclopentane-1-Carboxylic Acid. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:F501

b:76.0
occ:1.00
 F28 B:IF1501 0.0 76.0 1.0
C02 B:IF1501 1.4 68.6 1.0
F30 B:IF1501 2.3 69.0 1.0
F29 B:IF1501 2.3 65.7 1.0
C25 B:IF1501 2.4 56.2 1.0
C23 B:IF1501 3.1 51.6 1.0
CE1 B:TYR85 3.2 49.2 1.0
C24 B:IF1501 3.2 50.5 1.0
C03 B:IF1501 3.3 59.7 1.0
F31 B:IF1501 3.5 60.5 1.0
CZ B:TYR85 3.6 42.2 1.0
OH B:TYR85 3.8 55.7 1.0
CD1 B:TYR85 3.8 47.8 1.0
CG B:GLU235 4.3 60.7 1.0
CE2 B:TYR85 4.4 44.5 1.0
F32 B:IF1501 4.5 58.8 1.0
C20 B:IF1501 4.5 46.0 1.0
CG B:TYR85 4.6 39.3 1.0
C22 B:IF1501 4.7 40.4 1.0
CD2 B:TYR85 4.9 38.7 1.0
CB B:GLU235 5.0 56.2 1.0

Fluorine binding site 7 out of 15 in 7jx9

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Fluorine binding site 7 out of 15 in the The Crystal Structure of Human Ornithine Aminotransferase with An Intermediate Bound During Inactivation By (1S,3S)-3-Amino-4- (Hexafluoropropan-2-Ylidenyl)-Cyclopentane-1-Carboxylic Acid.


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 7 of The Crystal Structure of Human Ornithine Aminotransferase with An Intermediate Bound During Inactivation By (1S,3S)-3-Amino-4- (Hexafluoropropan-2-Ylidenyl)-Cyclopentane-1-Carboxylic Acid. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:F501

b:65.7
occ:1.00
 F29 B:IF1501 0.0 65.7 1.0
C02 B:IF1501 1.4 68.6 1.0
F30 B:IF1501 2.2 69.0 1.0
F28 B:IF1501 2.3 76.0 1.0
C25 B:IF1501 2.4 56.2 1.0
C24 B:IF1501 2.9 50.5 1.0
CG B:GLU235 3.0 60.7 1.0
C23 B:IF1501 3.2 51.6 1.0
C03 B:IF1501 3.5 59.7 1.0
C20 B:IF1501 3.6 46.0 1.0
CB B:GLU235 3.8 56.2 1.0
F31 B:IF1501 4.0 60.5 1.0
CE1 B:PHE177 4.1 37.6 1.0
N19 B:IF1501 4.2 34.7 1.0
CD1 B:PHE177 4.2 34.3 1.0
C21 B:IF1501 4.3 36.7 1.0
CD B:GLU235 4.3 70.0 1.0
CZ B:PHE177 4.4 27.3 1.0
C22 B:IF1501 4.4 40.4 1.0
OE2 B:GLU235 4.4 72.2 1.0
CA B:GLU235 4.5 48.3 1.0
CG B:PHE177 4.6 34.8 1.0
O26 B:IF1501 4.6 44.9 1.0
F32 B:IF1501 4.7 58.8 1.0
CE2 B:PHE177 4.8 36.1 1.0
C01 B:IF1501 4.8 41.9 1.0
CD2 B:PHE177 4.9 36.3 1.0

Fluorine binding site 8 out of 15 in 7jx9

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Fluorine binding site 8 out of 15 in the The Crystal Structure of Human Ornithine Aminotransferase with An Intermediate Bound During Inactivation By (1S,3S)-3-Amino-4- (Hexafluoropropan-2-Ylidenyl)-Cyclopentane-1-Carboxylic Acid.


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 8 of The Crystal Structure of Human Ornithine Aminotransferase with An Intermediate Bound During Inactivation By (1S,3S)-3-Amino-4- (Hexafluoropropan-2-Ylidenyl)-Cyclopentane-1-Carboxylic Acid. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:F501

b:69.0
occ:1.00
 F30 B:IF1501 0.0 69.0 1.0
C02 B:IF1501 1.4 68.6 1.0
F31 B:IF1501 2.2 60.5 1.0
F29 B:IF1501 2.2 65.7 1.0
F28 B:IF1501 2.3 76.0 1.0
C25 B:IF1501 2.3 56.2 1.0
C03 B:IF1501 2.6 59.7 1.0
CG B:GLU235 3.0 60.7 1.0
CA B:GLU235 3.0 48.3 1.0
CB B:GLU235 3.1 56.2 1.0
N B:GLU235 3.5 50.8 1.0
C24 B:IF1501 3.7 50.5 1.0
F32 B:IF1501 4.0 58.8 1.0
NH1 B:ARG413 4.1 56.9 1.0
C B:GLY234 4.2 47.7 1.0
C23 B:IF1501 4.3 51.6 1.0
O B:HOH711 4.4 42.2 1.0
CD B:GLU235 4.4 70.0 1.0
C B:GLU235 4.4 50.0 1.0
O B:GLY234 4.5 36.0 1.0
C20 B:IF1501 4.6 46.0 1.0
O B:GLU235 4.7 57.4 1.0
N19 B:IF1501 4.8 34.7 1.0
NE2 B:GLN266 4.9 57.2 1.0
CE1 B:TYR85 4.9 49.2 1.0
OE2 B:GLU235 4.9 72.2 1.0
CD1 B:TYR85 5.0 47.8 1.0

Fluorine binding site 9 out of 15 in 7jx9

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Fluorine binding site 9 out of 15 in the The Crystal Structure of Human Ornithine Aminotransferase with An Intermediate Bound During Inactivation By (1S,3S)-3-Amino-4- (Hexafluoropropan-2-Ylidenyl)-Cyclopentane-1-Carboxylic Acid.


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 9 of The Crystal Structure of Human Ornithine Aminotransferase with An Intermediate Bound During Inactivation By (1S,3S)-3-Amino-4- (Hexafluoropropan-2-Ylidenyl)-Cyclopentane-1-Carboxylic Acid. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:F501

b:60.5
occ:1.00
 F31 B:IF1501 0.0 60.5 1.0
C03 B:IF1501 1.4 59.7 1.0
F30 B:IF1501 2.2 69.0 1.0
C25 B:IF1501 2.3 56.2 1.0
F32 B:IF1501 2.4 58.8 1.0
C02 B:IF1501 2.8 68.6 1.0
NH1 B:ARG413 2.9 56.9 1.0
OE1 B:GLN266 3.0 57.4 1.0
NE2 B:GLN266 3.1 57.2 1.0
CD B:GLN266 3.3 60.2 1.0
F28 B:IF1501 3.5 76.0 1.0
CZ B:ARG413 3.6 62.4 1.0
C24 B:IF1501 3.7 50.5 1.0
NH2 B:ARG413 3.8 57.8 1.0
N B:GLU235 3.8 50.8 1.0
F29 B:IF1501 4.0 65.7 1.0
O B:HOH711 4.1 42.2 1.0
C B:GLY234 4.1 47.7 1.0
O10 B:IF1501 4.2 34.4 1.0
CD1 B:TYR85 4.2 47.8 1.0
CA B:GLU235 4.2 48.3 1.0
CA B:GLY234 4.4 41.7 1.0
N19 B:IF1501 4.4 34.7 1.0
NZ B:LYS292 4.5 41.8 1.0
C20 B:IF1501 4.5 46.0 1.0
O B:GLY234 4.6 36.0 1.0
CB B:GLU235 4.6 56.2 1.0
CE1 B:TYR85 4.7 49.2 1.0
NE B:ARG413 4.7 62.0 1.0
C23 B:IF1501 4.7 51.6 1.0
CG B:GLN266 4.7 43.6 1.0
CG B:TYR85 4.9 39.3 1.0

Fluorine binding site 10 out of 15 in 7jx9

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Fluorine binding site 10 out of 15 in the The Crystal Structure of Human Ornithine Aminotransferase with An Intermediate Bound During Inactivation By (1S,3S)-3-Amino-4- (Hexafluoropropan-2-Ylidenyl)-Cyclopentane-1-Carboxylic Acid.


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 10 of The Crystal Structure of Human Ornithine Aminotransferase with An Intermediate Bound During Inactivation By (1S,3S)-3-Amino-4- (Hexafluoropropan-2-Ylidenyl)-Cyclopentane-1-Carboxylic Acid. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:F501

b:58.8
occ:1.00
 F32 B:IF1501 0.0 58.8 1.0
C03 B:IF1501 1.4 59.7 1.0
NZ B:LYS292 2.2 41.8 1.0
C25 B:IF1501 2.3 56.2 1.0
F31 B:IF1501 2.4 60.5 1.0
C24 B:IF1501 2.8 50.5 1.0
N19 B:IF1501 3.1 34.7 1.0
C20 B:IF1501 3.2 46.0 1.0
NE2 B:GLN266 3.3 57.2 1.0
O10 B:IF1501 3.4 34.4 1.0
CE B:LYS292 3.5 42.1 1.0
CD B:GLN266 3.5 60.2 1.0
CB B:TYR85 3.5 41.2 1.0
OE1 B:GLN266 3.7 57.4 1.0
C02 B:IF1501 3.7 68.6 1.0
CG B:TYR85 3.9 39.3 1.0
CD1 B:TYR85 3.9 47.8 1.0
C23 B:IF1501 4.0 51.6 1.0
F30 B:IF1501 4.0 69.0 1.0
O B:TYR85 4.0 42.3 1.0
C18 B:IF1501 4.0 32.3 1.0
CG B:GLN266 4.4 43.6 1.0
CD B:LYS292 4.4 33.0 1.0
CA B:TYR85 4.4 38.2 1.0
F28 B:IF1501 4.5 76.0 1.0
C04 B:IF1501 4.5 31.9 1.0
NH2 B:ARG413 4.5 57.8 1.0
C21 B:IF1501 4.6 36.7 1.0
C B:TYR85 4.6 37.6 1.0
F29 B:IF1501 4.7 65.7 1.0
NH1 B:ARG413 4.7 56.9 1.0
CB B:GLN266 4.7 32.7 1.0
C09 B:IF1501 4.8 30.0 1.0
CE1 B:TYR85 4.8 49.2 1.0
CD2 B:TYR85 4.8 38.7 1.0
C22 B:IF1501 4.8 40.4 1.0

Reference:

A.Butrin, B.A.Beaupre, N.Kadamandla, P.Zhao, S.Shen, R.B.Silverman, G.R.Moran, D.Liu. Structural and Kinetic Analyses Reveal the Dual Inhibition Modes of Ornithine Aminotransferase By (1 S ,3 S )-3-Amino-4-(Hexafluoropropan-2-Ylidenyl) -Cyclopentane-1-Carboxylic Acid (Bcf 3 ). Acs Chem.Biol. 2020.
ISSN: ESSN 1554-8937
PubMed: 33316155
DOI: 10.1021/ACSCHEMBIO.0C00728
Page generated: Tue Jul 15 20:37:09 2025

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