Chlorine 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:

Fluorine

(F)

84 atoms

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 20; Page 3, Binding sites: 21 - 28;

Binding sites:

The binding sites of Chlorine 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 Chlorine atom.
In total 28 binding sites of Chlorine where determined in the Crystal Structure of Escherichia Coli Clpp Protease Complexed with Small Molecule Activator, ACP1-06, PDB code: 6nb1:
Jump to Chlorine binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Chlorine binding site 1 out of 28 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 Chlorine with other atoms in the Cl 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:Cl301 b:65.5 occ:0.48 CLB A:KHS301 0.0 65.5 0.5 CLB A:KHS301 0.2 65.6 0.3 CBB A:KHS301 1.6 65.0 0.3 CBB A:KHS301 1.7 65.0 0.5 CBA A:KHS301 2.6 65.7 0.3 CAZ A:KHS301 2.6 67.4 0.3 CBA A:KHS301 2.7 65.7 0.5 CAZ A:KHS301 2.7 67.4 0.5 SAV A:KHS301 3.1 77.4 0.3 SAV A:KHS301 3.2 77.2 0.5 CD2 A:LEU37 3.4 41.2 1.0 CD1 G:PHE63 3.5 39.6 1.0 CA G:PHE63 3.7 33.1 1.0 CAW A:KHS301 3.8 65.5 0.3 CAY A:KHS301 3.9 63.9 0.3 CG A:ARG36 3.9 46.9 1.0 CAW A:KHS301 4.0 65.5 0.5 CAY A:KHS301 4.0 63.7 0.5 CB G:ALA66 4.1 46.3 1.0 CB G:PHE63 4.1 29.1 1.0 O G:PHE63 4.2 32.8 1.0 CG G:PHE63 4.3 35.8 1.0 CZ A:ARG36 4.3 64.1 1.0 CAX A:KHS301 4.4 65.8 0.3 NH1 A:ARG36 4.4 60.8 1.0 CE1 G:PHE63 4.4 41.0 1.0 C G:PHE63 4.5 28.5 1.0 CAX A:KHS301 4.5 65.7 0.5 CG A:GLU40 4.5 53.5 1.0 N G:PHE63 4.5 30.4 1.0 NE A:ARG36 4.5 56.4 1.0 CG A:LEU37 4.6 34.2 1.0 O G:LEU62 4.7 33.1 1.0 NH2 A:ARG36 4.7 65.0 1.0 CD A:ARG36 4.8 50.4 1.0 O A:ARG36 4.8 31.6 1.0 CAU A:KHS301 4.9 65.4 0.3 C G:LEU62 4.9 35.5 1.0 CB A:ARG36 4.9 37.7 1.0 C A:ARG36 4.9 33.7 1.0 CA A:LEU37 5.0 26.0 1.0 CAU A:KHS301 5.0 65.3 0.5

Chlorine binding site 2 out of 28 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 Chlorine with other atoms in the Cl 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:Cl301 b:65.6 occ:0.33 CLB A:KHS301 0.0 65.6 0.3 CLB A:KHS301 0.2 65.5 0.5 CBB A:KHS301 1.7 65.0 0.3 CBB A:KHS301 1.9 65.0 0.5 CBA A:KHS301 2.7 65.7 0.3 CAZ A:KHS301 2.7 67.4 0.3 CBA A:KHS301 2.8 65.7 0.5 CAZ A:KHS301 2.9 67.4 0.5 SAV A:KHS301 3.2 77.4 0.3 SAV A:KHS301 3.3 77.2 0.5 CD1 G:PHE63 3.4 39.6 1.0 CD2 A:LEU37 3.4 41.2 1.0 CA G:PHE63 3.6 33.1 1.0 CG A:ARG36 3.8 46.9 1.0 CAW A:KHS301 4.0 65.5 0.3 CB G:PHE63 4.0 29.1 1.0 CAY A:KHS301 4.0 63.9 0.3 CAW A:KHS301 4.1 65.5 0.5 O G:PHE63 4.1 32.8 1.0 CG G:PHE63 4.1 35.8 1.0 CB G:ALA66 4.1 46.3 1.0 CAY A:KHS301 4.1 63.7 0.5 CE1 G:PHE63 4.3 41.0 1.0 C G:PHE63 4.3 28.5 1.0 CZ A:ARG36 4.4 64.1 1.0 N G:PHE63 4.4 30.4 1.0 NH1 A:ARG36 4.4 60.8 1.0 CAX A:KHS301 4.5 65.8 0.3 NE A:ARG36 4.5 56.4 1.0 O G:LEU62 4.6 33.1 1.0 CG A:LEU37 4.6 34.2 1.0 CAX A:KHS301 4.6 65.7 0.5 CG A:GLU40 4.6 53.5 1.0 NH2 A:ARG36 4.8 65.0 1.0 CD A:ARG36 4.8 50.4 1.0 C G:LEU62 4.9 35.5 1.0 O A:ARG36 4.9 31.6 1.0 CB A:ARG36 4.9 37.7 1.0 CAU A:KHS301 5.0 65.4 0.3 C A:ARG36 5.0 33.7 1.0 CA A:LEU37 5.0 26.0 1.0

Chlorine binding site 3 out of 28 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 Chlorine with other atoms in the Cl 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 B:Cl301 b:92.3 occ:0.46 CLB B:KHS301 0.0 92.3 0.5 CLB B:KHS301 0.2 91.9 0.3 CBB B:KHS301 1.6 79.2 0.3 CBB B:KHS301 1.7 79.3 0.5 CAZ B:KHS301 2.6 79.9 0.3 CBA B:KHS301 2.6 80.2 0.3 CBA B:KHS301 2.7 80.3 0.5 CAZ B:KHS301 2.7 80.2 0.5 SAV B:KHS301 3.0 94.3 0.3 SAV B:KHS301 3.2 93.9 0.5 NH1 B:ARG36 3.2 59.0 1.0 CD2 B:LEU37 3.3 45.3 1.0 CZ B:ARG36 3.6 59.8 1.0 CD1 A:PHE63 3.8 38.7 1.0 CAY B:KHS301 3.9 79.1 0.3 NH2 B:ARG36 3.9 64.0 1.0 CAW B:KHS301 3.9 79.0 0.3 CA A:PHE63 3.9 35.5 1.0 CAW B:KHS301 4.0 79.0 0.5 CAY B:KHS301 4.0 79.1 0.5 CB A:ALA66 4.0 53.2 1.0 CG B:ARG36 4.1 47.4 1.0 CG B:GLU40 4.1 59.2 1.0 O B:ARG36 4.2 35.3 1.0 NE B:ARG36 4.3 48.8 1.0 CB A:PHE63 4.4 33.0 1.0 CAX B:KHS301 4.4 80.2 0.3 CA B:LEU37 4.5 30.6 1.0 O A:PHE63 4.5 36.9 1.0 CAX B:KHS301 4.5 80.2 0.5 CG B:LEU37 4.5 38.1 1.0 CG A:PHE63 4.6 34.5 1.0 C B:ARG36 4.6 37.7 1.0 N A:PHE63 4.7 31.4 1.0 CAU B:KHS301 4.7 73.8 0.3 CD B:ARG36 4.7 48.7 1.0 CE1 A:PHE63 4.7 38.9 1.0 C A:PHE63 4.7 35.3 1.0 N B:LEU37 4.7 30.4 1.0 O A:LEU62 4.8 39.1 1.0 CAU B:KHS301 4.9 73.7 0.5 CB B:GLU40 4.9 43.8 1.0

Chlorine binding site 4 out of 28 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 Chlorine with other atoms in the Cl 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 B:Cl301 b:91.9 occ:0.30 CLB B:KHS301 0.0 91.9 0.3 CLB B:KHS301 0.2 92.3 0.5 CBB B:KHS301 1.7 79.2 0.3 CBB B:KHS301 1.8 79.3 0.5 CBA B:KHS301 2.7 80.2 0.3 CAZ B:KHS301 2.7 79.9 0.3 CBA B:KHS301 2.7 80.3 0.5 CAZ B:KHS301 2.8 80.2 0.5 SAV B:KHS301 3.1 94.3 0.3 NH1 B:ARG36 3.1 59.0 1.0 SAV B:KHS301 3.3 93.9 0.5 CD2 B:LEU37 3.4 45.3 1.0 CZ B:ARG36 3.5 59.8 1.0 CD1 A:PHE63 3.7 38.7 1.0 NH2 B:ARG36 3.8 64.0 1.0 CA A:PHE63 3.8 35.5 1.0 CAW B:KHS301 4.0 79.0 0.3 CAY B:KHS301 4.0 79.1 0.3 CG B:ARG36 4.0 47.4 1.0 CB A:ALA66 4.0 53.2 1.0 CAW B:KHS301 4.0 79.0 0.5 CAY B:KHS301 4.1 79.1 0.5 NE B:ARG36 4.2 48.8 1.0 O B:ARG36 4.2 35.3 1.0 CB A:PHE63 4.3 33.0 1.0 CG B:GLU40 4.3 59.2 1.0 O A:PHE63 4.4 36.9 1.0 CG A:PHE63 4.4 34.5 1.0 CAX B:KHS301 4.5 80.2 0.3 CA B:LEU37 4.5 30.6 1.0 CE1 A:PHE63 4.5 38.9 1.0 CG B:LEU37 4.6 38.1 1.0 C B:ARG36 4.6 37.7 1.0 CAX B:KHS301 4.6 80.2 0.5 CD B:ARG36 4.6 48.7 1.0 C A:PHE63 4.6 35.3 1.0 N A:PHE63 4.6 31.4 1.0 N B:LEU37 4.7 30.4 1.0 O A:LEU62 4.8 39.1 1.0 CAU B:KHS301 4.8 73.8 0.3 CAU B:KHS301 5.0 73.7 0.5

Chlorine binding site 5 out of 28 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 Chlorine with other atoms in the Cl 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 C:Cl301 b:94.3 occ:0.57 CLB C:KHS301 0.0 94.3 0.6 CLB C:KHS301 0.1 94.5 0.1 CBB C:KHS301 1.6 80.8 0.1 CBB C:KHS301 1.7 80.9 0.6 CAZ C:KHS301 2.5 78.9 0.1 CBA C:KHS301 2.6 79.6 0.1 CBA C:KHS301 2.7 79.5 0.6 CAZ C:KHS301 2.7 78.9 0.6 SAV C:KHS301 3.0 85.3 0.1 SAV C:KHS301 3.2 84.4 0.6 CD1 B:PHE63 3.3 41.5 1.0 CA B:PHE63 3.4 33.2 1.0 CAY C:KHS301 3.8 79.6 0.1 CAW C:KHS301 3.9 80.5 0.1 CB B:PHE63 3.9 33.0 1.0 CD1 C:LEU37 4.0 38.3 1.0 O B:PHE63 4.0 36.9 1.0 CAW C:KHS301 4.0 80.5 0.6 CG B:PHE63 4.0 34.2 1.0 CAY C:KHS301 4.0 79.8 0.6 CE1 B:PHE63 4.2 39.7 1.0 CB B:ALA66 4.2 49.2 1.0 C B:PHE63 4.2 34.4 1.0 N B:PHE63 4.3 32.9 1.0 CAX C:KHS301 4.4 80.5 0.1 O C:ARG36 4.4 37.0 1.0 CAX C:KHS301 4.5 80.8 0.6 O B:LEU62 4.5 32.4 1.0 CG C:ARG36 4.5 46.5 1.0 CG C:LEU37 4.6 39.1 1.0 CAU C:KHS301 4.7 73.3 0.1 CG C:GLU40 4.7 62.8 1.0 C B:LEU62 4.7 36.9 1.0 C C:ARG36 4.8 37.8 1.0 CA C:LEU37 4.9 29.3 1.0 CAU C:KHS301 4.9 72.8 0.6

Chlorine binding site 6 out of 28 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 Chlorine with other atoms in the Cl 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 C:Cl301 b:94.5 occ:0.13 CLB C:KHS301 0.0 94.5 0.1 CLB C:KHS301 0.1 94.3 0.6 CBB C:KHS301 1.7 80.8 0.1 CBB C:KHS301 1.8 80.9 0.6 CBA C:KHS301 2.7 79.6 0.1 CAZ C:KHS301 2.7 78.9 0.1 CBA C:KHS301 2.8 79.5 0.6 CAZ C:KHS301 2.9 78.9 0.6 SAV C:KHS301 3.1 85.3 0.1 CD1 B:PHE63 3.2 41.5 1.0 SAV C:KHS301 3.3 84.4 0.6 CA B:PHE63 3.4 33.2 1.0 CB B:PHE63 3.8 33.0 1.0 CD1 C:LEU37 3.9 38.3 1.0 CG B:PHE63 3.9 34.2 1.0 CAW C:KHS301 4.0 80.5 0.1 CAY C:KHS301 4.0 79.6 0.1 O B:PHE63 4.0 36.9 1.0 CE1 B:PHE63 4.1 39.7 1.0 CAW C:KHS301 4.1 80.5 0.6 CAY C:KHS301 4.1 79.8 0.6 C B:PHE63 4.2 34.4 1.0 CB B:ALA66 4.3 49.2 1.0 N B:PHE63 4.3 32.9 1.0 O C:ARG36 4.4 37.0 1.0 CG C:ARG36 4.4 46.5 1.0 CAX C:KHS301 4.5 80.5 0.1 CG C:LEU37 4.6 39.1 1.0 O B:LEU62 4.6 32.4 1.0 CAX C:KHS301 4.6 80.8 0.6 C C:ARG36 4.8 37.8 1.0 C B:LEU62 4.8 36.9 1.0 CG C:GLU40 4.8 62.8 1.0 CA C:LEU37 4.9 29.3 1.0 CAU C:KHS301 4.9 73.3 0.1 N C:LEU37 5.0 33.9 1.0

Chlorine binding site 7 out of 28 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 Chlorine with other atoms in the Cl 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 D:Cl301 b:72.6 occ:0.47 CLB D:KHS301 0.0 72.6 0.5 CLB D:KHS301 0.2 72.6 0.3 CBB D:KHS301 1.6 76.4 0.3 CBB D:KHS301 1.7 76.5 0.5 CAZ D:KHS301 2.6 78.2 0.3 CBA D:KHS301 2.7 75.0 0.3 CBA D:KHS301 2.7 75.1 0.5 CAZ D:KHS301 2.7 78.2 0.5 SAV D:KHS301 3.0 87.0 0.3 SAV D:KHS301 3.2 86.8 0.5 CA C:PHE63 3.4 34.5 1.0 OE1 D:GLU40 3.4 72.5 1.0 CD1 C:PHE63 3.5 41.4 1.0 O C:PHE63 3.9 37.5 1.0 CAY D:KHS301 3.9 78.7 0.3 NH1 D:ARG36 3.9 61.3 1.0 CB C:PHE63 3.9 35.4 1.0 CAW D:KHS301 4.0 75.5 0.3 CD2 D:LEU37 4.0 41.8 1.0 CAW D:KHS301 4.0 75.6 0.5 CG D:ARG36 4.0 47.4 1.0 CAY D:KHS301 4.0 78.8 0.5 OE2 D:GLU40 4.0 67.7 1.0 CD D:GLU40 4.1 67.9 1.0 C C:PHE63 4.1 38.2 1.0 CZ D:ARG36 4.1 64.8 1.0 CG C:PHE63 4.1 39.4 1.0 CB C:ALA66 4.1 49.1 1.0 O C:LEU62 4.2 37.6 1.0 N C:PHE63 4.2 33.7 1.0 CE1 C:PHE63 4.4 37.6 1.0 CAX D:KHS301 4.4 76.8 0.3 NH2 D:ARG36 4.5 65.0 1.0 CAX D:KHS301 4.5 76.8 0.5 NE D:ARG36 4.5 60.0 1.0 C C:LEU62 4.6 37.3 1.0 CAU D:KHS301 4.8 75.0 0.3 CD1 D:LEU37 4.8 43.3 1.0 CD D:ARG36 4.9 53.5 1.0 CAU D:KHS301 4.9 75.1 0.5 CG D:LEU37 5.0 39.3 1.0

Chlorine binding site 8 out of 28 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 Chlorine with other atoms in the Cl 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 D:Cl301 b:72.6 occ:0.29 CLB D:KHS301 0.0 72.6 0.3 CLB D:KHS301 0.2 72.6 0.5 CBB D:KHS301 1.7 76.4 0.3 CBB D:KHS301 1.8 76.5 0.5 CBA D:KHS301 2.7 75.0 0.3 CBA D:KHS301 2.7 75.1 0.5 CAZ D:KHS301 2.7 78.2 0.3 CAZ D:KHS301 2.9 78.2 0.5 SAV D:KHS301 3.2 87.0 0.3 CD1 C:PHE63 3.3 41.4 1.0 SAV D:KHS301 3.3 86.8 0.5 CA C:PHE63 3.3 34.5 1.0 OE1 D:GLU40 3.5 72.5 1.0 O C:PHE63 3.8 37.5 1.0 CB C:PHE63 3.9 35.4 1.0 NH1 D:ARG36 3.9 61.3 1.0 CG D:ARG36 3.9 47.4 1.0 CAW D:KHS301 4.0 75.5 0.3 CAY D:KHS301 4.0 78.7 0.3 CG C:PHE63 4.0 39.4 1.0 CAW D:KHS301 4.0 75.6 0.5 CZ D:ARG36 4.0 64.8 1.0 CD2 D:LEU37 4.0 41.8 1.0 C C:PHE63 4.1 38.2 1.0 OE2 D:GLU40 4.1 67.7 1.0 CAY D:KHS301 4.1 78.8 0.5 CD D:GLU40 4.1 67.9 1.0 CB C:ALA66 4.2 49.1 1.0 CE1 C:PHE63 4.2 37.6 1.0 N C:PHE63 4.2 33.7 1.0 O C:LEU62 4.3 37.6 1.0 NH2 D:ARG36 4.4 65.0 1.0 NE D:ARG36 4.4 60.0 1.0 CAX D:KHS301 4.5 76.8 0.3 CAX D:KHS301 4.6 76.8 0.5 C C:LEU62 4.6 37.3 1.0 CD D:ARG36 4.8 53.5 1.0 CD1 D:LEU37 4.9 43.3 1.0 CAU D:KHS301 4.9 75.0 0.3

Chlorine binding site 9 out of 28 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 Chlorine with other atoms in the Cl 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 E:Cl301 b:46.1 occ:0.37 CLB E:KHS301 0.0 46.1 0.4 CLB E:KHS301 0.2 46.1 0.5 CBB E:KHS301 1.6 53.2 0.5 CBB E:KHS301 1.7 53.0 0.4 CAZ E:KHS301 2.5 52.8 0.5 CBA E:KHS301 2.7 52.4 0.5 CBA E:KHS301 2.7 52.5 0.4 CAZ E:KHS301 2.7 52.9 0.4 SAV E:KHS301 2.9 45.8 0.5 SAV E:KHS301 3.2 46.6 0.4 CD1 E:LEU37 3.5 40.3 1.0 CA D:PHE63 3.7 34.4 1.0 CD1 D:PHE63 3.8 37.0 1.0 CAY E:KHS301 3.8 53.8 0.5 CAW E:KHS301 3.9 51.3 0.5 CAW E:KHS301 4.0 51.4 0.4 CAY E:KHS301 4.0 53.6 0.4 CG E:ARG36 4.1 45.0 1.0 CB D:PHE63 4.1 31.3 1.0 CG E:LEU37 4.2 34.8 1.0 CB D:ALA66 4.3 43.1 1.0 CAX E:KHS301 4.4 50.3 0.5 N D:PHE63 4.4 25.4 1.0 CG D:PHE63 4.4 34.8 1.0 CAX E:KHS301 4.5 50.5 0.4 NH1 E:ARG36 4.5 58.7 1.0 CG E:GLU40 4.6 55.1 1.0 CZ E:ARG36 4.6 62.0 1.0 O D:PHE63 4.7 36.6 1.0 O D:LEU62 4.7 38.2 1.0 CAU E:KHS301 4.7 50.6 0.5 C D:PHE63 4.7 37.9 1.0 CE1 D:PHE63 4.8 39.5 1.0 O E:ARG36 4.8 31.4 1.0 C D:LEU62 4.8 38.1 1.0 CA E:LEU37 4.8 24.9 1.0 NE E:ARG36 4.9 57.2 1.0 C E:ARG36 4.9 36.6 1.0 CAU E:KHS301 4.9 50.8 0.4 N E:LEU37 4.9 26.9 1.0

Chlorine binding site 10 out of 28 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 Chlorine with other atoms in the Cl 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 E:Cl301 b:46.1 occ:0.52 CLB E:KHS301 0.0 46.1 0.5 CLB E:KHS301 0.2 46.1 0.4 CBB E:KHS301 1.7 53.2 0.5 CBB E:KHS301 1.9 53.0 0.4 CBA E:KHS301 2.7 52.4 0.5 CAZ E:KHS301 2.7 52.8 0.5 CBA E:KHS301 2.8 52.5 0.4 CAZ E:KHS301 2.9 52.9 0.4 SAV E:KHS301 3.2 45.8 0.5 SAV E:KHS301 3.4 46.6 0.4 CD1 E:LEU37 3.5 40.3 1.0 CD1 D:PHE63 3.6 37.0 1.0 CA D:PHE63 3.7 34.4 1.0 CG E:ARG36 3.9 45.0 1.0 CAW E:KHS301 4.0 51.3 0.5 CAY E:KHS301 4.0 53.8 0.5 CB D:PHE63 4.0 31.3 1.0 CAW E:KHS301 4.1 51.4 0.4 CAY E:KHS301 4.2 53.6 0.4 CG E:LEU37 4.3 34.8 1.0 CG D:PHE63 4.3 34.8 1.0 CB D:ALA66 4.4 43.1 1.0 N D:PHE63 4.4 25.4 1.0 NH1 E:ARG36 4.4 58.7 1.0 CZ E:ARG36 4.5 62.0 1.0 CAX E:KHS301 4.5 50.3 0.5 CE1 D:PHE63 4.5 39.5 1.0 O D:PHE63 4.6 36.6 1.0 CAX E:KHS301 4.7 50.5 0.4 CG E:GLU40 4.7 55.1 1.0 C D:PHE63 4.7 37.9 1.0 NE E:ARG36 4.7 57.2 1.0 O E:ARG36 4.7 31.4 1.0 O D:LEU62 4.8 38.2 1.0 CA E:LEU37 4.8 24.9 1.0 C E:ARG36 4.8 36.6 1.0 N E:LEU37 4.9 26.9 1.0 C D:LEU62 4.9 38.1 1.0 CB E:ARG36 4.9 38.3 1.0 CD E:ARG36 4.9 48.6 1.0 NH2 E:ARG36 4.9 64.3 1.0 CAU E:KHS301 4.9 50.6 0.5

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