Fluorine in PDB 8qiy: Structure of Mycobacterium Abscessus Phosphopantetheine Adenylyltransferase in Complex with Inhibitor

Enzymatic activity of Structure of Mycobacterium Abscessus Phosphopantetheine Adenylyltransferase in Complex with Inhibitor

All present enzymatic activity of Structure of Mycobacterium Abscessus Phosphopantetheine Adenylyltransferase in Complex with Inhibitor:
2.7.7.3;

Protein crystallography data

The structure of Structure of Mycobacterium Abscessus Phosphopantetheine Adenylyltransferase in Complex with Inhibitor, PDB code: 8qiy was solved by S.E.Thomas, W.J.Mccarthy, A.G.Coyne, T.L.Blundell, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 65.21 / 1.51
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 76.307, 125.586, 119.243, 90, 90, 90
R / Rfree (%) 27.5 / 29.9

Fluorine Binding Sites:

The binding sites of Fluorine atom in the Structure of Mycobacterium Abscessus Phosphopantetheine Adenylyltransferase in Complex with Inhibitor (pdb code 8qiy). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 6 binding sites of Fluorine where determined in the Structure of Mycobacterium Abscessus Phosphopantetheine Adenylyltransferase in Complex with Inhibitor, PDB code: 8qiy:
Jump to Fluorine binding site number: 1; 2; 3; 4; 5; 6;

Fluorine binding site 1 out of 6 in 8qiy

Go back to Fluorine Binding Sites List in 8qiy
Fluorine binding site 1 out of 6 in the Structure of Mycobacterium Abscessus Phosphopantetheine Adenylyltransferase in Complex with Inhibitor


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Structure of Mycobacterium Abscessus Phosphopantetheine Adenylyltransferase in Complex with Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F201

b:65.9
occ:1.00
 F01 A:VCC201 0.0 65.9 1.0
C02 A:VCC201 1.3 42.8 1.0
O09 A:VCC201 2.0 31.5 1.0
F04 A:VCC201 2.0 48.2 1.0
F03 A:VCC201 2.1 72.0 1.0
C05 A:VCC201 2.2 55.4 1.0
C07 A:VCC201 2.6 47.6 1.0
C06 A:VCC201 2.6 56.5 1.0
CE1 A:HIS17 2.8 24.6 1.0
NE2 A:HIS17 2.9 27.4 1.0
CG2 A:THR14 3.2 23.9 1.0
OG1 A:THR14 3.3 22.9 1.0
N A:SER127 3.3 24.9 1.0
N12 A:VCC201 3.4 62.4 1.0
ND1 A:HIS17 3.6 19.6 1.0
OG A:SER127 3.6 23.8 1.0
CA A:SER126 3.6 27.0 1.0
CD2 A:HIS17 3.8 22.8 1.0
C A:SER126 3.9 24.4 1.0
O08 A:VCC201 3.9 69.8 1.0
CB A:THR14 3.9 22.8 1.0
C10 A:VCC201 4.0 62.4 1.0
O A:HOH316 4.0 32.6 1.0
CG A:HIS17 4.1 20.3 1.0
O A:VAL125 4.2 33.2 1.0
C13 A:VCC201 4.2 53.9 1.0
N11 A:VCC201 4.3 62.6 1.0
N19 A:VCC201 4.3 44.8 1.0
CA A:SER127 4.4 22.5 1.0
CB A:SER127 4.4 20.6 1.0
CB A:SER126 4.5 28.8 1.0
N A:SER126 4.5 23.9 1.0
C A:VAL125 4.6 29.5 1.0
C18 A:VCC201 4.7 49.5 1.0
O A:SER126 4.9 24.0 1.0
CG1 A:VAL125 4.9 30.7 1.0
N A:THR14 5.0 19.5 1.0

Fluorine binding site 2 out of 6 in 8qiy

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Fluorine binding site 2 out of 6 in the Structure of Mycobacterium Abscessus Phosphopantetheine Adenylyltransferase in Complex with Inhibitor


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Structure of Mycobacterium Abscessus Phosphopantetheine Adenylyltransferase in Complex with Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F201

b:72.0
occ:1.00
 F03 A:VCC201 0.0 72.0 1.0
C02 A:VCC201 1.3 42.8 1.0
F04 A:VCC201 2.0 48.2 1.0
F01 A:VCC201 2.1 65.9 1.0
C05 A:VCC201 2.3 55.4 1.0
OG1 A:THR14 2.3 22.9 1.0
NE2 A:HIS17 2.7 27.4 1.0
CD2 A:HIS17 2.7 22.8 1.0
N12 A:VCC201 2.8 62.4 1.0
CG A:HIS17 2.9 20.3 1.0
CE1 A:HIS17 2.9 24.6 1.0
ND1 A:HIS17 3.0 19.6 1.0
C13 A:VCC201 3.0 53.9 1.0
N A:HIS17 3.2 21.9 1.0
C06 A:VCC201 3.5 56.5 1.0
C18 A:VCC201 3.5 49.5 1.0
CB A:THR14 3.6 22.8 1.0
N19 A:VCC201 3.6 44.8 1.0
C14 A:VCC201 3.8 44.7 1.0
CG2 A:THR14 3.8 23.9 1.0
CB A:HIS17 3.8 19.1 1.0
C A:GLY16 3.8 25.8 1.0
CA A:HIS17 3.9 20.6 1.0
O09 A:VCC201 3.9 31.5 1.0
CA A:GLY16 4.0 24.4 1.0
N11 A:VCC201 4.0 62.6 1.0
C07 A:VCC201 4.2 47.6 1.0
N A:GLY16 4.4 22.6 1.0
C10 A:VCC201 4.4 62.4 1.0
C17 A:VCC201 4.4 46.1 1.0
CA A:THR14 4.5 21.2 1.0
N A:THR14 4.5 19.5 1.0
C15 A:VCC201 4.6 46.0 1.0
O A:VAL125 4.7 33.2 1.0
O A:GLY16 4.8 21.0 1.0
C A:THR14 4.8 21.2 1.0
O A:THR14 4.8 20.5 1.0
C16 A:VCC201 4.9 45.5 1.0

Fluorine binding site 3 out of 6 in 8qiy

Go back to Fluorine Binding Sites List in 8qiy
Fluorine binding site 3 out of 6 in the Structure of Mycobacterium Abscessus Phosphopantetheine Adenylyltransferase in Complex with Inhibitor


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Structure of Mycobacterium Abscessus Phosphopantetheine Adenylyltransferase in Complex with Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F201

b:48.2
occ:1.00
 F04 A:VCC201 0.0 48.2 1.0
C02 A:VCC201 1.2 42.8 1.0
F03 A:VCC201 2.0 72.0 1.0
F01 A:VCC201 2.0 65.9 1.0
C05 A:VCC201 2.3 55.4 1.0
N19 A:VCC201 2.5 44.8 1.0
OG1 A:THR14 2.7 22.9 1.0
O A:VAL125 2.8 33.2 1.0
N12 A:VCC201 3.0 62.4 1.0
C18 A:VCC201 3.2 49.5 1.0
C13 A:VCC201 3.4 53.9 1.0
C06 A:VCC201 3.4 56.5 1.0
C A:VAL125 3.4 29.5 1.0
CG1 A:VAL125 3.5 30.7 1.0
CG2 A:THR14 3.5 23.9 1.0
CB A:THR14 3.5 22.8 1.0
CA A:SER126 3.7 27.0 1.0
O09 A:VCC201 3.7 31.5 1.0
N A:SER126 3.9 23.9 1.0
C07 A:VCC201 4.0 47.6 1.0
CB A:VAL125 4.1 39.0 1.0
N11 A:VCC201 4.2 62.6 1.0
NE2 A:HIS17 4.2 27.4 1.0
CE1 A:HIS17 4.3 24.6 1.0
C A:SER126 4.4 24.4 1.0
C17 A:VCC201 4.4 46.1 1.0
CA A:VAL125 4.4 31.8 1.0
C10 A:VCC201 4.4 62.4 1.0
CA A:GLY16 4.4 24.4 1.0
N A:SER127 4.4 24.9 1.0
C14 A:VCC201 4.6 44.7 1.0
N A:HIS17 4.6 21.9 1.0
CD2 A:HIS17 4.6 22.8 1.0
ND1 A:HIS17 4.6 19.6 1.0
N A:GLY16 4.6 22.6 1.0
CB A:SER126 4.7 28.8 1.0
CG A:HIS17 4.8 20.3 1.0
C A:GLY16 4.9 25.8 1.0
CA A:THR14 4.9 21.2 1.0

Fluorine binding site 4 out of 6 in 8qiy

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Fluorine binding site 4 out of 6 in the Structure of Mycobacterium Abscessus Phosphopantetheine Adenylyltransferase in Complex with Inhibitor


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 4 of Structure of Mycobacterium Abscessus Phosphopantetheine Adenylyltransferase in Complex with Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
B:F201

b:51.8
occ:1.00
 F01 B:VCC201 0.0 51.8 1.0
C02 B:VCC201 1.3 39.5 1.0
F04 B:VCC201 2.1 66.9 1.0
N19 B:VCC201 2.2 42.0 1.0
F03 B:VCC201 2.2 57.9 1.0
C05 B:VCC201 2.4 52.6 1.0
O B:VAL125 2.4 35.0 1.0
C18 B:VCC201 3.1 45.3 1.0
C B:VAL125 3.1 35.2 1.0
N12 B:VCC201 3.1 60.4 1.0
OG1 B:THR14 3.2 24.2 1.0
CG1 B:VAL125 3.3 37.9 1.0
C13 B:VCC201 3.4 49.8 1.0
CA B:SER126 3.4 31.8 1.0
C06 B:VCC201 3.5 53.2 1.0
N B:SER126 3.6 28.8 1.0
O09 B:VCC201 3.9 53.2 1.0
NH2 B:ARG90 4.0 52.1 1.0
CG2 B:THR14 4.0 23.9 1.0
CB B:THR14 4.0 26.5 1.0
CB B:VAL125 4.1 37.7 1.0
C07 B:VCC201 4.1 39.3 1.0
CA B:VAL125 4.1 33.5 1.0
C B:SER126 4.2 26.7 1.0
N11 B:VCC201 4.2 56.1 1.0
C17 B:VCC201 4.2 41.0 1.0
CG2 B:VAL125 4.3 39.4 1.0
C10 B:VCC201 4.5 56.7 1.0
N B:SER127 4.5 29.4 1.0
CB B:SER126 4.5 36.0 1.0
CD B:ARG90 4.5 48.5 1.0
CE1 B:HIS17 4.6 27.4 1.0
NE2 B:HIS17 4.6 31.4 1.0
C14 B:VCC201 4.7 44.0 1.0
CA B:GLY16 4.7 23.1 1.0
O B:TYR122 4.8 31.9 1.0
N B:VAL125 4.9 29.5 1.0
CZ B:ARG90 4.9 56.6 1.0
N B:GLY16 5.0 24.7 1.0
ND1 B:HIS17 5.0 23.0 1.0
O B:SER126 5.0 29.6 1.0
N B:HIS17 5.0 21.4 1.0

Fluorine binding site 5 out of 6 in 8qiy

Go back to Fluorine Binding Sites List in 8qiy
Fluorine binding site 5 out of 6 in the Structure of Mycobacterium Abscessus Phosphopantetheine Adenylyltransferase in Complex with Inhibitor


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 5 of Structure of Mycobacterium Abscessus Phosphopantetheine Adenylyltransferase in Complex with Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
B:F201

b:57.9
occ:1.00
 F03 B:VCC201 0.0 57.9 1.0
C02 B:VCC201 1.3 39.5 1.0
OG1 B:THR14 2.1 24.2 1.0
F01 B:VCC201 2.2 51.8 1.0
F04 B:VCC201 2.2 66.9 1.0
C05 B:VCC201 2.3 52.6 1.0
CE1 B:HIS17 3.0 27.4 1.0
N12 B:VCC201 3.0 60.4 1.0
ND1 B:HIS17 3.0 23.0 1.0
NE2 B:HIS17 3.0 31.4 1.0
CG B:HIS17 3.1 21.7 1.0
CD2 B:HIS17 3.1 27.9 1.0
N B:HIS17 3.2 21.4 1.0
C13 B:VCC201 3.2 49.8 1.0
CB B:THR14 3.3 26.5 1.0
N19 B:VCC201 3.4 42.0 1.0
C18 B:VCC201 3.4 45.3 1.0
C06 B:VCC201 3.5 53.2 1.0
CG2 B:THR14 3.6 23.9 1.0
C B:GLY16 3.8 23.8 1.0
CA B:GLY16 3.9 23.1 1.0
CB B:HIS17 4.0 20.0 1.0
CA B:HIS17 4.0 20.6 1.0
C14 B:VCC201 4.1 44.0 1.0
N11 B:VCC201 4.1 56.1 1.0
N B:GLY16 4.2 24.7 1.0
C07 B:VCC201 4.2 39.3 1.0
CA B:THR14 4.3 23.2 1.0
N B:THR14 4.4 22.9 1.0
C17 B:VCC201 4.4 41.0 1.0
O09 B:VCC201 4.4 53.2 1.0
C10 B:VCC201 4.4 56.7 1.0
C B:THR14 4.6 23.4 1.0
O B:VAL125 4.6 35.0 1.0
O B:THR14 4.7 22.4 1.0
CG1 B:VAL125 4.7 37.9 1.0
O B:GLY16 4.8 23.1 1.0
C15 B:VCC201 4.9 40.7 1.0
O08 B:VCC201 5.0 54.3 1.0

Fluorine binding site 6 out of 6 in 8qiy

Go back to Fluorine Binding Sites List in 8qiy
Fluorine binding site 6 out of 6 in the Structure of Mycobacterium Abscessus Phosphopantetheine Adenylyltransferase in Complex with Inhibitor


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 6 of Structure of Mycobacterium Abscessus Phosphopantetheine Adenylyltransferase in Complex with Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
B:F201

b:66.9
occ:1.00
 F04 B:VCC201 0.0 66.9 1.0
C02 B:VCC201 1.3 39.5 1.0
F01 B:VCC201 2.1 51.8 1.0
F03 B:VCC201 2.2 57.9 1.0
C05 B:VCC201 2.3 52.6 1.0
O09 B:VCC201 2.5 53.2 1.0
C07 B:VCC201 2.7 39.3 1.0
C06 B:VCC201 2.8 53.2 1.0
CE1 B:HIS17 2.9 27.4 1.0
CG2 B:THR14 3.0 23.9 1.0
N B:SER127 3.1 29.4 1.0
OG1 B:THR14 3.2 24.2 1.0
NE2 B:HIS17 3.3 31.4 1.0
CA B:SER126 3.3 31.8 1.0
C B:SER126 3.5 26.7 1.0
OG B:SER127 3.5 28.3 1.0
O08 B:VCC201 3.6 54.3 1.0
ND1 B:HIS17 3.6 23.0 1.0
N12 B:VCC201 3.6 60.4 1.0
CB B:THR14 3.7 26.5 1.0
O B:VAL125 4.0 35.0 1.0
CA B:SER127 4.1 29.2 1.0
C10 B:VCC201 4.2 56.7 1.0
N B:SER126 4.2 28.8 1.0
CD2 B:HIS17 4.2 27.9 1.0
N19 B:VCC201 4.2 42.0 1.0
CB B:SER127 4.3 27.7 1.0
CG B:HIS17 4.3 21.7 1.0
CB B:SER126 4.4 36.0 1.0
C B:VAL125 4.4 35.2 1.0
O B:SER126 4.5 29.6 1.0
C13 B:VCC201 4.5 49.8 1.0
N11 B:VCC201 4.5 56.1 1.0
NH2 B:ARG90 4.7 52.1 1.0
C18 B:VCC201 4.7 45.3 1.0
N B:THR14 4.8 22.9 1.0
CA B:THR14 4.9 23.2 1.0

Reference:

W.J.Mccarthy, S.E.Thomas, T.Olaleye, J.A.Boland, R.A.Floto, G.Williams, T.L.Blundell, A.G.Coyne, C.Abell. A Fragment Based Competitive 19F Lb-uc(Nmr) Platform For Hotspot Directed Ligand Profiling. Angew.Chem.Int.Ed.Engl. 06846 2024.
ISSN: ESSN 1521-3773
PubMed: 38896426
DOI: 10.1002/ANIE.202406846
Page generated: Fri Aug 2 22:26:01 2024

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