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Bromine in PDB 7uw0: Crystal Structure of Human Clpp Protease in Complex with Tr-133

Enzymatic activity of Crystal Structure of Human Clpp Protease in Complex with Tr-133

All present enzymatic activity of Crystal Structure of Human Clpp Protease in Complex with Tr-133:
3.4.21.92;

Protein crystallography data

The structure of Crystal Structure of Human Clpp Protease in Complex with Tr-133, PDB code: 7uw0 was solved by M.F.Mabanglo, W.A.Houry, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 51.69 / 2.80
Space group I 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 105.66, 153.798, 133.208, 90, 107.03, 90
R / Rfree (%) 26 / 30.9

Bromine Binding Sites:

The binding sites of Bromine atom in the Crystal Structure of Human Clpp Protease in Complex with Tr-133 (pdb code 7uw0). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total 7 binding sites of Bromine where determined in the Crystal Structure of Human Clpp Protease in Complex with Tr-133, PDB code: 7uw0:
Jump to Bromine binding site number: 1; 2; 3; 4; 5; 6; 7;

Bromine binding site 1 out of 7 in 7uw0

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Bromine binding site 1 out of 7 in the Crystal Structure of Human Clpp Protease in Complex with Tr-133


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of Crystal Structure of Human Clpp Protease in Complex with Tr-133 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Br301

b:49.0
occ:1.00
BR21 A:P4I301 0.0 49.0 1.0
C20 A:P4I301 1.9 29.4 1.0
C22 A:P4I301 2.9 22.7 1.0
C19 A:P4I301 2.9 27.7 1.0
CD2 A:LEU79 3.6 25.1 1.0
CG A:ARG78 3.7 26.8 1.0
CB G:PHE105 3.7 16.0 1.0
CA G:PHE105 4.0 15.8 1.0
C23 A:P4I301 4.2 17.7 1.0
C18 A:P4I301 4.2 34.9 1.0
CG A:LEU79 4.3 21.9 1.0
O G:ALA101 4.3 20.1 1.0
N G:PHE105 4.3 18.6 1.0
CD1 G:PHE105 4.4 22.8 1.0
N A:LEU79 4.4 25.3 1.0
CB A:ARG78 4.4 30.4 1.0
O A:ILE75 4.5 24.5 1.0
CG G:PHE105 4.5 21.8 1.0
CG1 A:ILE75 4.5 15.8 1.0
CA A:LEU79 4.5 20.4 1.0
C A:ARG78 4.6 25.4 1.0
C17 A:P4I301 4.7 25.3 1.0
O A:ARG78 4.8 20.3 1.0
CD A:ARG78 4.8 16.9 1.0
CB A:LEU79 4.9 21.3 1.0
NE A:ARG78 5.0 33.6 1.0
CD1 A:ILE75 5.0 16.9 1.0

Bromine binding site 2 out of 7 in 7uw0

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Bromine binding site 2 out of 7 in the Crystal Structure of Human Clpp Protease in Complex with Tr-133


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 2 of Crystal Structure of Human Clpp Protease in Complex with Tr-133 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Br301

b:53.6
occ:1.00
BR21 B:P4I301 0.0 53.6 1.0
C20 B:P4I301 1.9 28.5 1.0
C22 B:P4I301 2.9 28.3 1.0
C19 B:P4I301 2.9 25.8 1.0
CD1 B:LEU79 3.6 29.8 1.0
CB A:PHE105 3.6 21.1 1.0
CG B:ARG78 3.9 29.1 1.0
CA A:PHE105 4.0 19.8 1.0
CD1 B:ILE75 4.2 23.9 1.0
C23 B:P4I301 4.2 26.5 1.0
C18 B:P4I301 4.2 30.1 1.0
O A:ALA101 4.2 24.2 1.0
N B:LEU79 4.3 30.8 1.0
N A:PHE105 4.4 21.4 1.0
CB B:ARG78 4.4 34.9 1.0
CG A:PHE105 4.4 30.3 1.0
CA B:LEU79 4.4 22.5 1.0
CD1 A:PHE105 4.4 28.7 1.0
C B:ARG78 4.4 30.0 1.0
O B:ARG78 4.6 25.3 1.0
O B:ILE75 4.6 27.0 1.0
C17 B:P4I301 4.7 28.3 1.0
CB B:LEU79 4.8 33.0 1.0
CG B:LEU79 4.8 35.3 1.0
NH1 B:ARG78 4.8 39.8 1.0
CG1 B:ILE75 4.9 23.4 1.0

Bromine binding site 3 out of 7 in 7uw0

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Bromine binding site 3 out of 7 in the Crystal Structure of Human Clpp Protease in Complex with Tr-133


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 3 of Crystal Structure of Human Clpp Protease in Complex with Tr-133 within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Br301

b:45.0
occ:1.00
BR21 C:P4I301 0.0 45.0 1.0
C20 C:P4I301 1.9 34.9 1.0
C22 C:P4I301 2.9 29.4 1.0
C19 C:P4I301 2.9 25.3 1.0
CD2 C:LEU79 3.6 19.3 1.0
CB B:PHE105 3.8 18.7 1.0
CG C:ARG78 3.9 26.6 1.0
CG C:LEU79 3.9 29.4 1.0
O B:ALA101 4.0 17.7 1.0
C23 C:P4I301 4.2 29.9 1.0
C18 C:P4I301 4.2 28.5 1.0
CA B:PHE105 4.2 22.8 1.0
NH1 C:ARG78 4.3 33.0 1.0
N C:LEU79 4.4 29.9 1.0
CD1 C:ILE75 4.4 15.4 1.0
N B:PHE105 4.4 23.4 1.0
CA C:LEU79 4.5 21.2 1.0
O C:ILE75 4.5 27.3 1.0
CB C:ARG78 4.5 23.0 1.0
CG1 C:ILE75 4.6 16.0 1.0
C C:ARG78 4.6 27.2 1.0
CD1 B:PHE105 4.6 29.9 1.0
CG B:PHE105 4.7 24.6 1.0
C17 C:P4I301 4.7 28.2 1.0
O C:ARG78 4.7 29.9 1.0
CB C:LEU79 4.8 23.6 1.0
C B:ALA101 5.0 16.4 1.0
CZ C:ARG78 5.0 42.3 1.0

Bromine binding site 4 out of 7 in 7uw0

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Bromine binding site 4 out of 7 in the Crystal Structure of Human Clpp Protease in Complex with Tr-133


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 4 of Crystal Structure of Human Clpp Protease in Complex with Tr-133 within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Br301

b:42.5
occ:1.00
BR21 D:P4I301 0.0 42.5 1.0
C20 D:P4I301 1.9 31.9 1.0
C22 D:P4I301 2.9 28.4 1.0
C19 D:P4I301 2.9 23.8 1.0
CG D:ARG78 3.7 25.5 1.0
CG D:LEU79 3.7 29.0 1.0
CB C:PHE105 3.9 18.9 1.0
N D:LEU79 4.0 22.9 1.0
C23 D:P4I301 4.2 24.2 1.0
CA D:LEU79 4.2 26.3 1.0
CA C:PHE105 4.2 18.3 1.0
C18 D:P4I301 4.2 23.5 1.0
CG1 D:ILE75 4.3 15.6 1.0
CD2 D:LEU79 4.3 29.7 1.0
C D:ARG78 4.3 20.8 1.0
CB D:ARG78 4.3 23.6 1.0
CD1 C:PHE105 4.4 26.8 1.0
O C:ALA101 4.4 12.8 1.0
CD1 D:LEU79 4.4 32.9 1.0
O D:ILE75 4.4 22.9 1.0
CB D:LEU79 4.5 22.6 1.0
N C:PHE105 4.5 21.3 1.0
O D:ARG78 4.6 21.2 1.0
CG C:PHE105 4.6 20.4 1.0
C17 D:P4I301 4.7 27.6 1.0
NH1 D:ARG78 4.8 21.4 1.0
CD D:ARG78 4.9 25.1 1.0
CD1 D:ILE75 4.9 15.4 1.0

Bromine binding site 5 out of 7 in 7uw0

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Bromine binding site 5 out of 7 in the Crystal Structure of Human Clpp Protease in Complex with Tr-133


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 5 of Crystal Structure of Human Clpp Protease in Complex with Tr-133 within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Br301

b:39.1
occ:1.00
BR21 E:P4I301 0.0 39.1 1.0
C20 E:P4I301 1.9 32.6 1.0
C22 E:P4I301 2.9 29.9 1.0
C19 E:P4I301 2.9 26.3 1.0
CD E:ARG78 3.6 32.0 1.0
CD2 E:LEU79 3.6 21.1 1.0
CB D:PHE105 3.6 16.4 1.0
CA D:PHE105 4.0 17.3 1.0
O D:ALA101 4.0 14.0 1.0
C23 E:P4I301 4.2 24.4 1.0
C18 E:P4I301 4.2 36.1 1.0
N D:PHE105 4.2 16.0 1.0
CG E:LEU79 4.3 20.8 1.0
N E:LEU79 4.4 19.6 1.0
NE E:ARG78 4.4 33.8 1.0
O E:ILE75 4.4 23.5 1.0
CG D:PHE105 4.5 19.0 1.0
CD1 D:PHE105 4.5 22.9 1.0
CG1 E:ILE75 4.5 18.3 1.0
CA E:LEU79 4.6 15.9 1.0
C E:ARG78 4.6 21.0 1.0
CB E:ARG78 4.6 22.7 1.0
O E:ARG78 4.7 16.5 1.0
CG E:ARG78 4.7 21.6 1.0
C17 E:P4I301 4.7 30.4 1.0
CG E:GLU82 4.8 23.8 1.0
CD1 E:ILE75 4.9 27.8 1.0
CB E:LEU79 4.9 24.2 1.0
C D:LEU104 4.9 21.3 1.0
C D:ALA101 4.9 15.9 1.0

Bromine binding site 6 out of 7 in 7uw0

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Bromine binding site 6 out of 7 in the Crystal Structure of Human Clpp Protease in Complex with Tr-133


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 6 of Crystal Structure of Human Clpp Protease in Complex with Tr-133 within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Br301

b:53.0
occ:1.00
BR21 F:P4I301 0.0 53.0 1.0
C20 F:P4I301 1.9 26.1 1.0
C22 F:P4I301 2.9 27.1 1.0
C19 F:P4I301 2.9 21.9 1.0
CD2 F:LEU79 3.5 14.2 1.0
CG F:ARG78 3.5 24.1 1.0
CB E:PHE105 3.7 13.5 1.0
CA E:PHE105 4.1 14.8 1.0
CD1 E:PHE105 4.2 23.8 1.0
C23 F:P4I301 4.2 30.6 1.0
C18 F:P4I301 4.2 24.7 1.0
CB F:ARG78 4.2 19.0 1.0
O E:ALA101 4.3 16.2 1.0
N F:LEU79 4.3 18.8 1.0
C F:ARG78 4.4 17.2 1.0
CG F:LEU79 4.4 18.6 1.0
N E:PHE105 4.4 17.5 1.0
CA F:LEU79 4.4 14.3 1.0
CG E:PHE105 4.4 16.8 1.0
O F:ARG78 4.5 16.3 1.0
O F:ILE75 4.5 15.8 1.0
CD1 F:ILE75 4.6 15.2 1.0
CG1 F:ILE75 4.6 8.7 1.0
CD F:ARG78 4.7 23.1 1.0
C17 F:P4I301 4.7 24.4 1.0
NH1 F:ARG78 4.9 23.7 1.0
CA F:ARG78 5.0 22.9 1.0
NE F:ARG78 5.0 39.1 1.0
CB F:LEU79 5.0 15.6 1.0

Bromine binding site 7 out of 7 in 7uw0

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Bromine binding site 7 out of 7 in the Crystal Structure of Human Clpp Protease in Complex with Tr-133


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 7 of Crystal Structure of Human Clpp Protease in Complex with Tr-133 within 5.0Å range:
probe atom residue distance (Å) B Occ
G:Br301

b:39.4
occ:1.00
BR21 G:P4I301 0.0 39.4 1.0
C20 G:P4I301 1.9 26.9 1.0
C22 G:P4I301 2.9 25.0 1.0
C19 G:P4I301 2.9 30.3 1.0
CB F:PHE105 3.5 23.4 1.0
CD2 G:LEU79 3.7 21.4 1.0
CG G:ARG78 3.9 20.7 1.0
CA F:PHE105 3.9 23.1 1.0
C23 G:P4I301 4.2 25.6 1.0
CD1 F:PHE105 4.2 23.0 1.0
N F:PHE105 4.2 24.0 1.0
C18 G:P4I301 4.2 34.0 1.0
O F:ALA101 4.3 18.6 1.0
CG G:LEU79 4.3 26.1 1.0
CG F:PHE105 4.3 25.6 1.0
N G:LEU79 4.5 24.6 1.0
O G:ARG78 4.5 20.6 1.0
C G:ARG78 4.5 23.4 1.0
NH1 G:ARG78 4.5 30.6 1.0
CB G:ARG78 4.5 20.4 1.0
CA G:LEU79 4.6 20.1 1.0
O G:ILE75 4.6 20.7 1.0
CG1 G:ILE75 4.6 20.3 1.0
C17 G:P4I301 4.7 26.6 1.0
CG G:GLU82 4.8 26.9 1.0
CD1 G:ILE75 4.9 20.2 1.0
C F:LEU104 5.0 23.4 1.0
CZ G:ARG78 5.0 31.0 1.0
CB G:LEU79 5.0 27.0 1.0

Reference:

M.F.Mabanglo, K.S.Wong, M.M.Barghash, E.Leung, S.H.W.Chuang, A.Ardalan, E.M.Majaesic, C.J.Wong, S.Zhang, H.Lang, D.S.Karanewsky, A.A.Iwanowicz, L.M.Graves, E.J.Iwanowicz, A.C.Gingras, W.A.Houry. Potent Clpp Agonists with Anticancer Properties Bind with Improved Structural Complementarity and Alter the Mitochondrial N-Terminome. Structure 2022.
ISSN: ISSN 0969-2126
PubMed: 36586405
DOI: 10.1016/J.STR.2022.12.002
Page generated: Mon Jul 7 11:52:14 2025

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