Fluorine in PDB 6nb1: Crystal Structure of Escherichia Coli Clpp Protease Complexed with Small Molecule Activator, ACP1-06

All present enzymatic activity of Crystal Structure of Escherichia Coli Clpp Protease Complexed with Small Molecule Activator, ACP1-06:
3.4.21.92;

The structure of Crystal Structure of Escherichia Coli Clpp Protease Complexed with Small Molecule Activator, ACP1-06, PDB code: 6nb1 was solved by M.F.Mabanglo, W.A.Houry, B.T.Eger, S.Bryson, E.F.Pai, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.00 / 1.90
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	190.985, 101.094, 155.194, 90.00, 98.29, 90.00
R / Rfree (%)	20.9 / 24.4

The structure of Crystal Structure of Escherichia Coli Clpp Protease Complexed with Small Molecule Activator, ACP1-06 also contains other interesting chemical elements:

Chlorine

(Cl)

28 atoms

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 20; Page 3, Binding sites: 21 - 30; Page 4, Binding sites: 31 - 40; Page 5, Binding sites: 41 - 50; Page 6, Binding sites: 51 - 60; Page 7, Binding sites: 61 - 70; Page 8, Binding sites: 71 - 80; Page 9, Binding sites: 81 - 84;

Binding sites:

The binding sites of Fluorine atom in the Crystal Structure of Escherichia Coli Clpp Protease Complexed with Small Molecule Activator, ACP1-06 (pdb code 6nb1). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 84 binding sites of Fluorine where determined in the Crystal Structure of Escherichia Coli Clpp Protease Complexed with Small Molecule Activator, ACP1-06, PDB code: 6nb1:
Jump to Fluorine binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Fluorine binding site 1 out of 84 in the Crystal Structure of Escherichia Coli Clpp Protease Complexed with Small Molecule Activator, ACP1-06


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 Escherichia Coli Clpp Protease Complexed with Small Molecule Activator, ACP1-06 within 5.0Å range: probe atom residue distance (Å) B Occ A:F301 b:58.3 occ:0.48 FAA A:KHS301 0.0 58.3 0.5 CAC A:KHS301 1.3 52.6 0.5 FAB A:KHS301 2.1 56.2 0.5 FAD A:KHS301 2.2 67.9 0.5 CAF A:KHS301 2.2 54.3 0.5 CAE A:KHS301 2.5 60.4 0.5 CAG A:KHS301 3.5 54.1 0.5 NAI A:KHS301 3.9 66.0 0.5 CAH A:KHS301 4.6 59.0 0.5 CZ A:PHE126 4.7 28.9 1.0 CAJ A:KHS301 4.7 63.3 0.5

Fluorine binding site 2 out of 84 in the Crystal Structure of Escherichia Coli Clpp Protease Complexed with Small Molecule Activator, ACP1-06


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 Escherichia Coli Clpp Protease Complexed with Small Molecule Activator, ACP1-06 within 5.0Å range: probe atom residue distance (Å) B Occ A:F301 b:36.8 occ:0.33 FAA A:KHS301 0.0 36.8 0.3 CAC A:KHS301 1.3 40.4 0.3 FAD A:KHS301 2.1 33.9 0.3 FAB A:KHS301 2.2 32.4 0.3 CAF A:KHS301 2.2 46.9 0.3 CAE A:KHS301 2.7 48.9 0.3 CG G:PHE96 3.0 37.1 1.0 CB G:PHE96 3.2 28.6 1.0 CD1 G:PHE96 3.3 40.3 1.0 CD2 A:LEU128 3.3 36.6 1.0 CAG A:KHS301 3.4 48.9 0.3 CD1 A:LEU128 3.5 30.4 1.0 CD2 G:PHE96 3.5 40.3 1.0 CE1 G:PHE96 4.0 46.6 1.0 NAI A:KHS301 4.0 54.6 0.3 CG A:LEU128 4.1 27.2 1.0 CE2 G:PHE96 4.2 45.4 1.0 CZ G:PHE96 4.4 42.7 1.0 O G:ASP92 4.4 19.5 1.0 CA G:THR93 4.6 19.6 1.0 CAH A:KHS301 4.6 56.3 0.3 CA G:PHE96 4.7 25.5 1.0 OH A:TYR76 4.8 36.8 1.0 CE2 A:TYR76 4.8 32.8 1.0 CAJ A:KHS301 4.8 62.0 0.3 OG1 G:THR93 4.8 23.0 1.0 C G:ASP92 5.0 25.4 1.0

Fluorine binding site 3 out of 84 in the Crystal Structure of Escherichia Coli Clpp Protease Complexed with Small Molecule Activator, ACP1-06


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 Escherichia Coli Clpp Protease Complexed with Small Molecule Activator, ACP1-06 within 5.0Å range: probe atom residue distance (Å) B Occ A:F301 b:67.9 occ:0.48 FAD A:KHS301 0.0 67.9 0.5 CAC A:KHS301 1.3 52.6 0.5 FAB A:KHS301 2.1 56.2 0.5 FAA A:KHS301 2.2 58.3 0.5 CAF A:KHS301 2.2 54.3 0.5 CAG A:KHS301 3.0 54.1 0.5 CAE A:KHS301 3.1 60.4 0.5 CE2 A:PHE126 4.1 32.9 1.0 CZ A:PHE126 4.1 28.9 1.0 CE1 A:TYR74 4.2 40.9 1.0 CAH A:KHS301 4.2 59.0 0.5 NAI A:KHS301 4.3 66.0 0.5 OH A:TYR74 4.7 47.6 1.0 CAJ A:KHS301 4.7 63.3 0.5 OG A:SER102 4.8 25.2 1.0 CZ A:TYR74 4.9 43.0 1.0 OAK A:KHS301 4.9 62.9 0.3

Fluorine binding site 4 out of 84 in the Crystal Structure of Escherichia Coli Clpp Protease Complexed with Small Molecule Activator, ACP1-06


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 Escherichia Coli Clpp Protease Complexed with Small Molecule Activator, ACP1-06 within 5.0Å range: probe atom residue distance (Å) B Occ A:F301 b:33.9 occ:0.33 FAD A:KHS301 0.0 33.9 0.3 CAC A:KHS301 1.3 40.4 0.3 FAA A:KHS301 2.1 36.8 0.3 FAB A:KHS301 2.2 32.4 0.3 CAF A:KHS301 2.2 46.9 0.3 CAG A:KHS301 3.0 48.9 0.3 CAE A:KHS301 3.1 48.9 0.3 CE2 A:TYR76 3.4 32.8 1.0 OH A:TYR76 3.6 36.8 1.0 OG1 G:THR93 3.6 23.0 1.0 CD1 A:LEU128 3.9 30.4 1.0 CZ A:TYR76 4.0 37.3 1.0 CD2 G:LEU62 4.1 29.7 1.0 CG2 G:THR93 4.2 23.3 1.0 CAH A:KHS301 4.3 56.3 0.3 CB G:THR93 4.3 22.4 1.0 NAI A:KHS301 4.3 54.6 0.3 CA G:THR93 4.4 19.6 1.0 CD2 A:TYR76 4.4 30.7 1.0 CD1 G:PHE96 4.6 40.3 1.0 CD1 G:LEU62 4.8 29.4 1.0 CAJ A:KHS301 4.8 62.0 0.3 CG G:PHE96 4.8 37.1 1.0 CB G:PHE96 4.8 28.6 1.0 CD2 A:LEU128 4.8 36.6 1.0 CG G:LEU62 4.9 29.7 1.0 CG1 G:VAL58 4.9 21.2 1.0 CG A:LEU128 5.0 27.2 1.0

Fluorine binding site 5 out of 84 in the Crystal Structure of Escherichia Coli Clpp Protease Complexed with Small Molecule Activator, ACP1-06


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 Escherichia Coli Clpp Protease Complexed with Small Molecule Activator, ACP1-06 within 5.0Å range: probe atom residue distance (Å) B Occ A:F301 b:56.2 occ:0.48 FAB A:KHS301 0.0 56.2 0.5 CAC A:KHS301 1.3 52.6 0.5 FAA A:KHS301 2.1 58.3 0.5 FAD A:KHS301 2.1 67.9 0.5 CAF A:KHS301 2.1 54.3 0.5 CAG A:KHS301 2.6 54.1 0.5 CZ A:PHE126 2.9 28.9 1.0 CE2 A:PHE126 3.2 32.9 1.0 CAE A:KHS301 3.3 60.4 0.5 CE1 A:PHE126 3.6 25.0 1.0 CAH A:KHS301 3.9 59.0 0.5 CD2 A:LEU203 4.0 35.0 1.0 CD2 A:PHE126 4.0 25.9 1.0 CD1 A:LEU203 4.4 37.0 1.0 CD1 A:PHE126 4.4 32.5 1.0 NAI A:KHS301 4.5 66.0 0.5 CG A:PHE126 4.6 23.9 1.0 CAJ A:KHS301 4.7 63.3 0.5 CG A:LEU203 4.7 37.5 1.0 OAK A:KHS301 4.9 62.9 0.3

Fluorine binding site 6 out of 84 in the Crystal Structure of Escherichia Coli Clpp Protease Complexed with Small Molecule Activator, ACP1-06


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 Escherichia Coli Clpp Protease Complexed with Small Molecule Activator, ACP1-06 within 5.0Å range: probe atom residue distance (Å) B Occ A:F301 b:32.4 occ:0.33 FAB A:KHS301 0.0 32.4 0.3 CAC A:KHS301 1.4 40.4 0.3 FAD A:KHS301 2.2 33.9 0.3 FAA A:KHS301 2.2 36.8 0.3 CAF A:KHS301 2.2 46.9 0.3 CAG A:KHS301 2.6 48.9 0.3 CD1 G:PHE96 3.0 40.3 1.0 CB G:PHE96 3.2 28.6 1.0 CG G:PHE96 3.3 37.1 1.0 CAE A:KHS301 3.5 48.9 0.3 CG2 G:ILE97 3.6 28.5 1.0 CA G:THR93 3.9 19.6 1.0 CG2 G:THR93 3.9 23.3 1.0 CE1 G:PHE96 3.9 46.6 1.0 CD2 G:LEU62 3.9 29.7 1.0 CAH A:KHS301 3.9 56.3 0.3 O G:THR93 3.9 22.6 1.0 N G:ILE97 4.1 25.9 1.0 CB G:THR93 4.3 22.4 1.0 OG1 G:THR93 4.3 23.0 1.0 C G:THR93 4.4 24.7 1.0 CA G:PHE96 4.4 25.5 1.0 CD2 G:PHE96 4.4 40.3 1.0 C G:PHE96 4.5 34.1 1.0 NAI A:KHS301 4.6 54.6 0.3 O G:ASP92 4.7 19.5 1.0 CA G:ILE97 4.7 26.6 1.0 CAJ A:KHS301 4.8 62.0 0.3 CB G:ILE97 4.8 27.8 1.0 OH A:TYR76 4.8 36.8 1.0 CZ G:PHE96 4.9 42.7 1.0 N G:THR93 4.9 20.7 1.0

Fluorine binding site 7 out of 84 in the Crystal Structure of Escherichia Coli Clpp Protease Complexed with Small Molecule Activator, ACP1-06


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 Escherichia Coli Clpp Protease Complexed with Small Molecule Activator, ACP1-06 within 5.0Å range: probe atom residue distance (Å) B Occ B:F301 b:72.5 occ:0.46 FAA B:KHS301 0.0 72.5 0.5 CAC B:KHS301 1.3 64.5 0.5 FAB B:KHS301 2.1 62.8 0.5 FAD B:KHS301 2.2 69.5 0.5 CAF B:KHS301 2.2 59.7 0.5 CAE B:KHS301 2.6 64.6 0.5 CAG B:KHS301 3.5 57.3 0.5 NAI B:KHS301 4.0 70.4 0.5 CAH B:KHS301 4.6 61.7 0.5 CZ B:PHE126 4.7 30.8 1.0 CAJ B:KHS301 4.7 68.4 0.5

Fluorine binding site 8 out of 84 in the Crystal Structure of Escherichia Coli Clpp Protease Complexed with Small Molecule Activator, ACP1-06


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 Escherichia Coli Clpp Protease Complexed with Small Molecule Activator, ACP1-06 within 5.0Å range: probe atom residue distance (Å) B Occ B:F301 b:42.9 occ:0.30 FAA B:KHS301 0.0 42.9 0.3 CAC B:KHS301 1.3 43.9 0.3 FAD B:KHS301 2.1 38.8 0.3 FAB B:KHS301 2.2 40.7 0.3 CAF B:KHS301 2.2 52.7 0.3 CAE B:KHS301 2.6 51.9 0.3 CG A:PHE96 3.1 39.7 1.0 CD2 A:PHE96 3.2 46.0 1.0 CB A:PHE96 3.2 31.2 1.0 CAG B:KHS301 3.4 53.4 0.3 CD2 B:LEU128 3.5 34.2 1.0 CD1 B:LEU128 3.7 29.8 0.8 CD1 A:PHE96 3.9 39.6 1.0 CE2 A:PHE96 3.9 54.0 1.0 NAI B:KHS301 4.0 60.2 0.3 CG B:LEU128 4.2 29.4 1.0 CA A:THR93 4.4 25.6 1.0 O A:ASP92 4.4 25.4 1.0 CE1 A:PHE96 4.5 45.2 1.0 CZ A:PHE96 4.6 48.7 1.0 CAH B:KHS301 4.6 59.3 0.3 OG1 A:THR93 4.6 24.1 1.0 CA A:PHE96 4.7 30.7 1.0 OH B:TYR76 4.8 40.8 1.0 CE2 B:TYR76 4.8 35.0 1.0 CAJ B:KHS301 4.8 65.6 0.3 C A:ASP92 4.9 30.9 1.0 N A:THR93 4.9 26.0 1.0

Fluorine binding site 9 out of 84 in the Crystal Structure of Escherichia Coli Clpp Protease Complexed with Small Molecule Activator, ACP1-06


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 Escherichia Coli Clpp Protease Complexed with Small Molecule Activator, ACP1-06 within 5.0Å range: probe atom residue distance (Å) B Occ B:F301 b:69.5 occ:0.46 FAD B:KHS301 0.0 69.5 0.5 CAC B:KHS301 1.4 64.5 0.5 FAB B:KHS301 2.1 62.8 0.5 FAA B:KHS301 2.2 72.5 0.5 CAF B:KHS301 2.2 59.7 0.5 CAG B:KHS301 3.0 57.3 0.5 CAE B:KHS301 3.1 64.6 0.5 O B:HOH402 3.2 46.3 1.0 CE1 B:TYR74 4.0 41.8 1.0 CE2 B:PHE126 4.1 35.4 1.0 CAH B:KHS301 4.3 61.7 0.5 CZ B:PHE126 4.3 30.8 1.0 NAI B:KHS301 4.3 70.4 0.5 OH B:TYR74 4.5 53.5 1.0 OG B:SER102 4.6 31.4 1.0 CZ B:TYR74 4.7 45.4 1.0 CAJ B:KHS301 4.8 68.4 0.5 CD1 B:TYR74 4.9 38.6 1.0

Fluorine binding site 10 out of 84 in the Crystal Structure of Escherichia Coli Clpp Protease Complexed with Small Molecule Activator, ACP1-06


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 10 of Crystal Structure of Escherichia Coli Clpp Protease Complexed with Small Molecule Activator, ACP1-06 within 5.0Å range: probe atom residue distance (Å) B Occ B:F301 b:38.8 occ:0.30 FAD B:KHS301 0.0 38.8 0.3 CAC B:KHS301 1.3 43.9 0.3 FAA B:KHS301 2.1 42.9 0.3 FAB B:KHS301 2.2 40.7 0.3 CAF B:KHS301 2.2 52.7 0.3 CAG B:KHS301 3.0 53.4 0.3 CAE B:KHS301 3.1 51.9 0.3 OG1 A:THR93 3.5 24.1 1.0 CE2 B:TYR76 3.5 35.0 1.0 OH B:TYR76 3.7 40.8 1.0 CD2 A:LEU62 4.0 34.6 1.0 CZ B:TYR76 4.0 35.0 1.0 CG2 A:THR93 4.1 25.6 1.0 CB A:THR93 4.1 25.1 1.0 CD1 B:LEU128 4.2 29.8 0.8 CA A:THR93 4.3 25.6 1.0 CAH B:KHS301 4.3 59.3 0.3 NAI B:KHS301 4.3 60.2 0.3 CD2 B:TYR76 4.5 28.0 1.0 CD2 A:PHE96 4.6 46.0 1.0 CAJ B:KHS301 4.8 65.6 0.3 CG A:LEU62 4.8 35.2 1.0 CB A:PHE96 4.8 31.2 1.0 CG1 A:VAL58 4.9 23.6 1.0 CD1 A:LEU62 4.9 31.3 1.0 CG A:PHE96 4.9 39.7 1.0

M.F.Mabanglo, W.A.Houry. Molecular Basis of Clpp Activation By Small Molecules To Be Published.