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Fluorine in PDB 6vg0: Crystal Structure of Human Cytosolic Isocitrate Dehydrogenase (IDH1) R132H Mutant in Complex with Nadph and Agi-15056

Enzymatic activity of Crystal Structure of Human Cytosolic Isocitrate Dehydrogenase (IDH1) R132H Mutant in Complex with Nadph and Agi-15056

All present enzymatic activity of Crystal Structure of Human Cytosolic Isocitrate Dehydrogenase (IDH1) R132H Mutant in Complex with Nadph and Agi-15056:
1.1.1.42;

Protein crystallography data

The structure of Crystal Structure of Human Cytosolic Isocitrate Dehydrogenase (IDH1) R132H Mutant in Complex with Nadph and Agi-15056, PDB code: 6vg0 was solved by A.Padyana, L.Jin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 41.20 / 2.66
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 196.770, 89.160, 90.750, 90.00, 90.00, 90.00
R / Rfree (%) 20.6 / 26.4

Fluorine Binding Sites:

The binding sites of Fluorine atom in the Crystal Structure of Human Cytosolic Isocitrate Dehydrogenase (IDH1) R132H Mutant in Complex with Nadph and Agi-15056 (pdb code 6vg0). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 9 binding sites of Fluorine where determined in the Crystal Structure of Human Cytosolic Isocitrate Dehydrogenase (IDH1) R132H Mutant in Complex with Nadph and Agi-15056, PDB code: 6vg0:
Jump to Fluorine binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9;

Fluorine binding site 1 out of 9 in 6vg0

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Fluorine binding site 1 out of 9 in the Crystal Structure of Human Cytosolic Isocitrate Dehydrogenase (IDH1) R132H Mutant in Complex with Nadph and Agi-15056


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Crystal Structure of Human Cytosolic Isocitrate Dehydrogenase (IDH1) R132H Mutant in Complex with Nadph and Agi-15056 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:F501

b:33.3
occ:0.44
 F27 B:QWM501 0.0 33.3 0.4
C22 B:QWM501 1.0 33.1 0.6
C26 B:QWM501 1.4 28.1 0.4
C20 B:QWM501 1.9 28.2 0.6
C24 B:QWM501 2.1 34.8 0.6
F28 B:QWM501 2.2 30.6 0.4
F29 B:QWM501 2.2 26.5 0.4
C19 B:QWM501 2.4 30.1 0.4
N18 B:QWM501 2.7 33.8 0.4
C19 B:QWM501 3.1 30.9 0.6
CA B:ASP273 3.3 25.8 1.0
C11 B:QWM501 3.3 35.3 0.6
OD1 B:ASP273 3.4 21.2 1.0
NE2 B:GLN277 3.4 36.9 0.6
CB B:ASP273 3.5 34.9 1.0
O B:ASP273 3.5 35.7 1.0
N18 B:QWM501 3.6 34.9 0.6
C20 B:QWM501 3.6 29.5 0.4
CG B:ASP273 3.8 30.9 1.0
C B:ASP273 3.8 36.0 1.0
CD1 B:ILE251 4.0 30.3 1.0
OE1 B:GLN277 4.0 39.7 0.4
C11 B:QWM501 4.1 35.2 0.4
CG B:GLN277 4.1 35.9 0.6
CD B:GLN277 4.3 38.4 0.6
CD B:GLN277 4.3 34.7 0.4
C26 B:QWM501 4.4 27.9 0.6
NE2 B:GLN277 4.4 29.9 0.4
CG1 B:ILE251 4.5 30.3 1.0
N B:ASP273 4.5 28.7 1.0
C06 B:QWM501 4.5 36.8 0.6
F29 B:QWM501 4.6 32.1 0.6
CB B:VAL276 4.7 29.4 1.0
C22 B:QWM501 4.7 30.6 0.4
F28 B:QWM501 4.8 25.7 0.6
N01 B:QWM501 4.8 36.7 0.4
N05 B:QWM501 4.8 36.5 0.6
CG2 B:VAL255 4.8 35.9 1.0
CG1 B:VAL276 4.8 40.4 1.0
CG1 A:VAL276 4.8 36.6 1.0
OD2 B:ASP273 4.8 41.1 1.0
O B:TYR272 4.9 27.0 1.0
C06 B:QWM501 4.9 37.0 0.4
C24 B:QWM501 4.9 33.0 0.4

Fluorine binding site 2 out of 9 in 6vg0

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Fluorine binding site 2 out of 9 in the Crystal Structure of Human Cytosolic Isocitrate Dehydrogenase (IDH1) R132H Mutant in Complex with Nadph and Agi-15056


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Crystal Structure of Human Cytosolic Isocitrate Dehydrogenase (IDH1) R132H Mutant in Complex with Nadph and Agi-15056 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:F501

b:30.7
occ:0.56
 F27 B:QWM501 0.0 30.7 0.6
C22 B:QWM501 0.9 30.6 0.4
C26 B:QWM501 1.4 27.9 0.6
C20 B:QWM501 1.9 29.5 0.4
C24 B:QWM501 1.9 33.0 0.4
F28 B:QWM501 2.2 25.7 0.6
F29 B:QWM501 2.2 32.1 0.6
C19 B:QWM501 2.4 30.9 0.6
N18 B:QWM501 2.7 34.9 0.6
C19 B:QWM501 3.1 30.1 0.4
C11 B:QWM501 3.1 35.2 0.4
CA A:ASP273 3.3 30.7 1.0
OD1 A:ASP273 3.3 29.6 1.0
O A:ASP273 3.4 33.3 1.0
CB A:ASP273 3.4 28.4 1.0
N18 B:QWM501 3.5 33.8 0.4
C20 B:QWM501 3.6 28.2 0.6
NE2 A:GLN277 3.6 36.3 0.4
CG A:ASP273 3.7 29.6 1.0
C A:ASP273 3.8 32.4 1.0
NE2 A:GLN277 3.8 38.3 0.6
OE1 A:GLN277 3.9 33.3 0.4
CD1 A:ILE251 4.1 23.5 1.0
C11 B:QWM501 4.1 35.3 0.6
CD A:GLN277 4.1 36.1 0.4
CG1 A:VAL276 4.1 36.6 1.0
CB A:VAL276 4.3 35.9 1.0
C06 B:QWM501 4.3 37.0 0.4
C26 B:QWM501 4.4 28.1 0.4
CG1 A:ILE251 4.5 26.5 1.0
N A:ASP273 4.5 27.5 1.0
CG A:GLN277 4.6 37.4 0.6
CD A:GLN277 4.6 36.7 0.6
N05 B:QWM501 4.6 37.1 0.4
F29 B:QWM501 4.7 26.5 0.4
C22 B:QWM501 4.7 33.1 0.6
OD2 A:ASP273 4.8 34.9 1.0
F28 B:QWM501 4.8 30.6 0.4
N01 B:QWM501 4.8 37.6 0.6
O A:TYR272 4.8 28.7 1.0
CG1 A:VAL255 4.9 30.3 1.0
C24 B:QWM501 4.9 34.8 0.6
C06 B:QWM501 4.9 36.8 0.6

Fluorine binding site 3 out of 9 in 6vg0

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Fluorine binding site 3 out of 9 in the Crystal Structure of Human Cytosolic Isocitrate Dehydrogenase (IDH1) R132H Mutant in Complex with Nadph and Agi-15056


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Crystal Structure of Human Cytosolic Isocitrate Dehydrogenase (IDH1) R132H Mutant in Complex with Nadph and Agi-15056 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:F501

b:30.6
occ:0.44
 F28 B:QWM501 0.0 30.6 0.4
C26 B:QWM501 1.4 28.1 0.4
C20 B:QWM501 1.8 28.2 0.6
C22 B:QWM501 2.0 33.1 0.6
F27 B:QWM501 2.2 33.3 0.4
F29 B:QWM501 2.2 26.5 0.4
C19 B:QWM501 2.4 30.1 0.4
C19 B:QWM501 2.9 30.9 0.6
OD1 B:ASP273 3.0 21.2 1.0
C20 B:QWM501 3.2 29.5 0.4
CG1 B:ILE251 3.2 30.3 1.0
N18 B:QWM501 3.2 33.8 0.4
C24 B:QWM501 3.2 34.8 0.6
F29 B:QWM501 3.4 32.1 0.6
OH A:TYR272 3.4 30.7 1.0
CG1 A:VAL276 3.4 36.6 1.0
CD1 B:ILE251 3.5 30.3 1.0
CE2 A:TYR272 3.6 31.6 1.0
CG2 A:VAL276 3.6 33.9 1.0
C26 B:QWM501 3.8 27.9 0.6
CZ A:TYR272 3.8 28.4 1.0
CG B:ASP273 3.8 30.9 1.0
N18 B:QWM501 3.9 34.9 0.6
CB A:VAL276 4.0 35.9 1.0
C11 B:QWM501 4.0 35.3 0.6
C22 B:QWM501 4.4 30.6 0.4
CB B:ASP273 4.4 34.9 1.0
C11 B:QWM501 4.4 35.2 0.4
CA B:ASP273 4.5 25.8 1.0
CB B:ILE251 4.6 24.0 1.0
F28 B:QWM501 4.6 25.7 0.6
CD2 A:TYR272 4.6 24.7 1.0
OD2 B:ASP273 4.7 41.1 1.0
F27 B:QWM501 4.8 30.7 0.6
CG2 B:VAL255 4.9 35.9 1.0
C24 B:QWM501 4.9 33.0 0.4
CG2 B:ILE251 4.9 26.2 1.0
CE1 A:TYR272 5.0 24.8 1.0

Fluorine binding site 4 out of 9 in 6vg0

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Fluorine binding site 4 out of 9 in the Crystal Structure of Human Cytosolic Isocitrate Dehydrogenase (IDH1) R132H Mutant in Complex with Nadph and Agi-15056


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 4 of Crystal Structure of Human Cytosolic Isocitrate Dehydrogenase (IDH1) R132H Mutant in Complex with Nadph and Agi-15056 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:F501

b:25.7
occ:0.56
 F28 B:QWM501 0.0 25.7 0.6
C26 B:QWM501 1.4 27.9 0.6
C20 B:QWM501 1.7 29.5 0.4
C22 B:QWM501 1.8 30.6 0.4
F27 B:QWM501 2.2 30.7 0.6
F29 B:QWM501 2.2 32.1 0.6
C19 B:QWM501 2.4 30.9 0.6
C19 B:QWM501 2.8 30.1 0.4
C24 B:QWM501 3.0 33.0 0.4
OD1 A:ASP273 3.0 29.6 1.0
C20 B:QWM501 3.2 28.2 0.6
N18 B:QWM501 3.2 34.9 0.6
CG1 A:ILE251 3.3 26.5 1.0
F29 B:QWM501 3.5 26.5 0.4
CE2 B:TYR272 3.5 24.6 1.0
OH B:TYR272 3.5 24.6 1.0
CG1 B:VAL276 3.5 40.4 1.0
CD1 A:ILE251 3.7 23.5 1.0
N18 B:QWM501 3.7 33.8 0.4
C11 B:QWM501 3.7 35.2 0.4
CG A:ASP273 3.8 29.6 1.0
C26 B:QWM501 3.8 28.1 0.4
CZ B:TYR272 3.8 20.0 1.0
CG2 B:VAL276 3.9 29.2 1.0
CB B:VAL276 4.1 29.4 1.0
CB A:ASP273 4.4 28.4 1.0
C22 B:QWM501 4.4 33.1 0.6
C11 B:QWM501 4.4 35.3 0.6
CD2 B:TYR272 4.5 22.0 1.0
OD2 A:ASP273 4.5 34.9 1.0
CA A:ASP273 4.6 30.7 1.0
F28 B:QWM501 4.6 30.6 0.4
CB A:ILE251 4.7 20.6 1.0
F27 B:QWM501 4.8 33.3 0.4
C24 B:QWM501 4.9 34.8 0.6
CG1 A:VAL255 5.0 30.3 1.0
CG2 A:ILE251 5.0 23.4 1.0

Fluorine binding site 5 out of 9 in 6vg0

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Fluorine binding site 5 out of 9 in the Crystal Structure of Human Cytosolic Isocitrate Dehydrogenase (IDH1) R132H Mutant in Complex with Nadph and Agi-15056


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 5 of Crystal Structure of Human Cytosolic Isocitrate Dehydrogenase (IDH1) R132H Mutant in Complex with Nadph and Agi-15056 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:F501

b:26.5
occ:0.44
 F29 B:QWM501 0.0 26.5 0.4
C26 B:QWM501 1.4 28.1 0.4
C20 B:QWM501 1.8 28.2 0.6
F28 B:QWM501 2.2 30.6 0.4
F27 B:QWM501 2.2 33.3 0.4
C19 B:QWM501 2.4 30.1 0.4
C22 B:QWM501 2.6 33.1 0.6
C20 B:QWM501 2.8 29.5 0.4
OD1 B:ASP273 2.8 21.2 1.0
C19 B:QWM501 2.9 30.9 0.6
F29 B:QWM501 3.1 32.1 0.6
CD2 B:TYR272 3.3 22.0 1.0
CA B:ASP273 3.3 25.8 1.0
C26 B:QWM501 3.3 27.9 0.6
CE2 B:TYR272 3.4 24.6 1.0
F28 B:QWM501 3.5 25.7 0.6
N18 B:QWM501 3.6 33.8 0.4
CE2 A:TYR272 3.6 31.6 1.0
CG B:ASP273 3.7 30.9 1.0
C24 B:QWM501 3.8 34.8 0.6
N B:ASP273 3.8 28.7 1.0
CB B:ASP273 3.9 34.9 1.0
O B:TYR272 4.0 27.0 1.0
N18 B:QWM501 4.0 34.9 0.6
C B:TYR272 4.1 26.1 1.0
C22 B:QWM501 4.1 30.6 0.4
OH A:TYR272 4.2 30.7 1.0
O B:ASP273 4.3 35.7 1.0
CB B:VAL276 4.3 29.4 1.0
C B:ASP273 4.3 36.0 1.0
CG B:TYR272 4.4 24.2 1.0
CZ A:TYR272 4.4 28.4 1.0
C11 B:QWM501 4.4 35.3 0.6
CG2 B:VAL276 4.5 29.2 1.0
CD2 A:TYR272 4.6 24.7 1.0
CG1 B:VAL276 4.6 40.4 1.0
CZ B:TYR272 4.6 20.0 1.0
C11 B:QWM501 4.7 35.2 0.4
F27 B:QWM501 4.7 30.7 0.6
C24 B:QWM501 4.9 33.0 0.4
OD2 B:ASP273 4.9 41.1 1.0
CB B:TYR272 4.9 28.3 1.0

Fluorine binding site 6 out of 9 in 6vg0

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Fluorine binding site 6 out of 9 in the Crystal Structure of Human Cytosolic Isocitrate Dehydrogenase (IDH1) R132H Mutant in Complex with Nadph and Agi-15056


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 6 of Crystal Structure of Human Cytosolic Isocitrate Dehydrogenase (IDH1) R132H Mutant in Complex with Nadph and Agi-15056 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:F501

b:32.1
occ:0.56
 F29 B:QWM501 0.0 32.1 0.6
C26 B:QWM501 1.4 27.9 0.6
C20 B:QWM501 1.6 29.5 0.4
F28 B:QWM501 2.2 25.7 0.6
F27 B:QWM501 2.2 30.7 0.6
C22 B:QWM501 2.3 30.6 0.4
C19 B:QWM501 2.4 30.9 0.6
C19 B:QWM501 2.7 30.1 0.4
OD1 A:ASP273 2.8 29.6 1.0
C20 B:QWM501 2.8 28.2 0.6
F29 B:QWM501 3.1 26.5 0.4
C26 B:QWM501 3.2 28.1 0.4
CD2 A:TYR272 3.3 24.7 1.0
CE2 A:TYR272 3.3 31.6 1.0
F28 B:QWM501 3.4 30.6 0.4
CA A:ASP273 3.5 30.7 1.0
N18 B:QWM501 3.6 34.9 0.6
C24 B:QWM501 3.6 33.0 0.4
CE2 B:TYR272 3.6 24.6 1.0
CG A:ASP273 3.7 29.6 1.0
N18 B:QWM501 3.8 33.8 0.4
CB A:VAL276 3.9 35.9 1.0
CB A:ASP273 4.0 28.4 1.0
CG1 A:VAL276 4.0 36.6 1.0
CG2 A:VAL276 4.0 33.9 1.0
N A:ASP273 4.1 27.5 1.0
O A:TYR272 4.1 28.7 1.0
C22 B:QWM501 4.1 33.1 0.6
C11 B:QWM501 4.2 35.2 0.4
C A:TYR272 4.3 28.7 1.0
OH B:TYR272 4.4 24.6 1.0
O A:ASP273 4.4 33.3 1.0
CD2 B:TYR272 4.4 22.0 1.0
CG A:TYR272 4.4 30.1 1.0
C A:ASP273 4.5 32.4 1.0
CZ A:TYR272 4.5 28.4 1.0
CZ B:TYR272 4.5 20.0 1.0
F27 B:QWM501 4.6 33.3 0.4
C11 B:QWM501 4.7 35.3 0.6
OD2 A:ASP273 4.9 34.9 1.0
C24 B:QWM501 4.9 34.8 0.6

Fluorine binding site 7 out of 9 in 6vg0

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Fluorine binding site 7 out of 9 in the Crystal Structure of Human Cytosolic Isocitrate Dehydrogenase (IDH1) R132H Mutant in Complex with Nadph and Agi-15056


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 7 of Crystal Structure of Human Cytosolic Isocitrate Dehydrogenase (IDH1) R132H Mutant in Complex with Nadph and Agi-15056 within 5.0Å range:
probe atom residue distance (Å) B Occ
C:F501

b:40.9
occ:0.47
 F27 C:QWM501 0.0 40.9 0.5
C26 C:QWM501 1.4 42.4 0.5
F28 C:QWM501 2.2 37.1 0.5
F29 C:QWM501 2.2 46.9 0.5
C19 C:QWM501 2.4 47.3 0.5
N18 C:QWM501 2.7 53.2 0.5
CA C:ASP273 3.3 31.0 1.0
OD1 C:ASP273 3.3 33.5 1.0
OE1 C:GLN277 3.3 47.9 0.6
CB C:ASP273 3.5 33.5 1.0
O C:ASP273 3.5 43.7 1.0
C20 C:QWM501 3.6 44.8 0.5
CG C:ASP273 3.7 31.0 1.0
C C:ASP273 3.8 36.1 1.0
CG1 C:VAL276 4.0 48.7 1.0
C11 C:QWM501 4.0 55.2 0.5
CB C:VAL276 4.1 46.0 1.0
CD1 C:ILE251 4.2 34.2 1.0
CD C:GLN277 4.2 54.7 0.6
NE2 C:GLN277 4.3 55.7 0.4
CG C:GLN277 4.4 51.5 0.4
CG1 C:ILE251 4.5 37.7 1.0
N C:ASP273 4.5 33.4 1.0
NE2 C:GLN277 4.5 55.8 0.6
C22 C:QWM501 4.7 43.0 0.5
CD C:GLN277 4.7 56.0 0.4
N01 C:QWM501 4.7 55.1 0.5
O C:TYR272 4.8 37.1 1.0
OD2 C:ASP273 4.8 41.2 1.0
C24 C:QWM501 4.9 49.8 0.5
C06 C:QWM501 4.9 55.1 0.5
CG2 C:VAL276 4.9 41.0 1.0

Fluorine binding site 8 out of 9 in 6vg0

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Fluorine binding site 8 out of 9 in the Crystal Structure of Human Cytosolic Isocitrate Dehydrogenase (IDH1) R132H Mutant in Complex with Nadph and Agi-15056


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 8 of Crystal Structure of Human Cytosolic Isocitrate Dehydrogenase (IDH1) R132H Mutant in Complex with Nadph and Agi-15056 within 5.0Å range:
probe atom residue distance (Å) B Occ
C:F501

b:37.1
occ:0.47
 F28 C:QWM501 0.0 37.1 0.5
C26 C:QWM501 1.4 42.4 0.5
F29 C:QWM501 2.2 46.9 0.5
F27 C:QWM501 2.2 40.9 0.5
C19 C:QWM501 2.4 47.3 0.5
OD1 C:ASP273 2.9 33.5 1.0
CG1 C:ILE251 3.1 37.7 1.0
N18 C:QWM501 3.2 53.2 0.5
C20 C:QWM501 3.2 44.8 0.5
CD1 C:ILE251 3.5 34.2 1.0
CG C:ASP273 3.6 31.0 1.0
CB C:ASP273 4.2 33.5 1.0
CB C:ILE251 4.4 32.5 1.0
C11 C:QWM501 4.4 55.2 0.5
OD2 C:ASP273 4.4 41.2 1.0
C22 C:QWM501 4.4 43.0 0.5
CA C:ASP273 4.5 31.0 1.0
CG2 C:ILE251 4.6 42.8 1.0
C24 C:QWM501 4.9 49.8 0.5

Fluorine binding site 9 out of 9 in 6vg0

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Fluorine binding site 9 out of 9 in the Crystal Structure of Human Cytosolic Isocitrate Dehydrogenase (IDH1) R132H Mutant in Complex with Nadph and Agi-15056


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 9 of Crystal Structure of Human Cytosolic Isocitrate Dehydrogenase (IDH1) R132H Mutant in Complex with Nadph and Agi-15056 within 5.0Å range:
probe atom residue distance (Å) B Occ
C:F501

b:46.9
occ:0.47
 F29 C:QWM501 0.0 46.9 0.5
C26 C:QWM501 1.4 42.4 0.5
F28 C:QWM501 2.2 37.1 0.5
F27 C:QWM501 2.2 40.9 0.5
C19 C:QWM501 2.4 47.3 0.5
OD1 C:ASP273 2.7 33.5 1.0
C20 C:QWM501 2.8 44.8 0.5
CE2 C:TYR272 3.3 41.1 1.0
CD2 C:TYR272 3.3 33.4 1.0
N18 C:QWM501 3.6 53.2 0.5
CA C:ASP273 3.7 31.0 1.0
CG C:ASP273 3.7 31.0 1.0
C22 C:QWM501 4.1 43.0 0.5
CB C:ASP273 4.1 33.5 1.0
N C:ASP273 4.2 33.4 1.0
CB C:VAL276 4.2 46.0 1.0
CG2 C:VAL276 4.3 41.0 1.0
CG1 C:VAL276 4.3 48.7 1.0
O C:TYR272 4.4 37.1 1.0
CZ C:TYR272 4.4 37.8 1.0
C C:TYR272 4.5 35.8 1.0
CG C:TYR272 4.5 35.3 1.0
C11 C:QWM501 4.7 55.2 0.5
C C:ASP273 4.7 36.1 1.0
O C:ASP273 4.8 43.7 1.0
OD2 C:ASP273 4.8 41.2 1.0
C24 C:QWM501 4.9 49.8 0.5

Reference:

Z.Konteatis, E.Artin, B.Nicolay, K.Straley, A.K.Padyana, L.Jin, Y.Chen, R.Narayaraswamy, S.Tong, F.Wang, D.Zhou, D.Cui, Z.Cai, Z.Luo, C.Fang, H.Tang, X.Lv, R.Nagaraja, H.Yang, S.M.Su, Z.Sui, L.Dang, K.Yen, J.Popovici-Muller, P.Codega, C.Campos, I.K.Mellinghoff, S.Biller. Vorasidenib (Ag-881): A First-in-Class, Brain-Penetrant Dual Inhibitor of Mutant IDH1 and 2 For Treatment of Glioma Acs Med.Chem.Lett. 2020.
ISSN: ISSN 1948-5875
DOI: 10.1021/ACSMEDCHEMLETT.9B00509
Page generated: Tue Jul 15 16:38:28 2025

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