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Chlorine in PDB 7uvr: Crystal Structure of Human Clpp Protease in Complex with Tr-65

Enzymatic activity of Crystal Structure of Human Clpp Protease in Complex with Tr-65

All present enzymatic activity of Crystal Structure of Human Clpp Protease in Complex with Tr-65:
3.4.21.92;

Protein crystallography data

The structure of Crystal Structure of Human Clpp Protease in Complex with Tr-65, PDB code: 7uvr 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) 29.35 / 2.86
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 142.171, 152.515, 104.268, 90, 118.1, 90
R / Rfree (%) 20.3 / 25.3

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Human Clpp Protease in Complex with Tr-65 (pdb code 7uvr). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 7 binding sites of Chlorine where determined in the Crystal Structure of Human Clpp Protease in Complex with Tr-65, PDB code: 7uvr:
Jump to Chlorine binding site number: 1; 2; 3; 4; 5; 6; 7;

Chlorine binding site 1 out of 7 in 7uvr

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Chlorine binding site 1 out of 7 in the Crystal Structure of Human Clpp Protease in Complex with Tr-65


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 Human Clpp Protease in Complex with Tr-65 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl301

b:61.4
occ:1.00
 CL1 A:PJF301 0.0 61.4 1.0
C18 A:PJF301 1.7 47.5 1.0
C19 A:PJF301 2.7 46.1 1.0
C17 A:PJF301 2.7 46.5 1.0
CB G:PHE105 3.4 37.8 1.0
CG A:ARG78 3.5 47.8 1.0
CD1 G:PHE105 3.7 43.4 1.0
CA G:PHE105 3.8 44.9 1.0
C20 A:PJF301 4.0 46.2 1.0
C16 A:PJF301 4.0 46.2 1.0
CG G:PHE105 4.0 43.2 1.0
CD2 A:LEU79 4.2 46.5 1.0
NH1 A:ARG78 4.2 51.8 1.0
N G:PHE105 4.3 44.1 1.0
CB A:ARG78 4.4 53.7 1.0
C15 A:PJF301 4.5 46.3 1.0
CZ A:ARG78 4.5 61.9 1.0
CG A:GLU82 4.5 46.0 1.0
CG A:LEU79 4.5 48.8 1.0
N A:LEU79 4.6 47.2 1.0
C A:ARG78 4.6 49.3 1.0
O A:ARG78 4.6 48.9 1.0
CA A:LEU79 4.6 41.4 1.0
CD A:ARG78 4.7 56.7 1.0
NE A:ARG78 4.7 68.1 1.0
CG1 A:ILE75 4.7 38.4 1.0
O G:ALA101 4.7 41.7 1.0
CE1 G:PHE105 4.9 42.6 1.0
O A:ILE75 5.0 45.1 1.0

Chlorine binding site 2 out of 7 in 7uvr

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Chlorine binding site 2 out of 7 in the Crystal Structure of Human Clpp Protease in Complex with Tr-65


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 Human Clpp Protease in Complex with Tr-65 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl301

b:64.8
occ:1.00
 CL1 B:PJF301 0.0 64.8 1.0
C18 B:PJF301 1.7 52.9 1.0
C17 B:PJF301 2.7 52.8 1.0
C19 B:PJF301 2.7 48.7 1.0
CD2 B:LEU79 3.7 47.6 1.0
CB A:PHE105 3.7 41.8 1.0
CA A:PHE105 3.8 41.9 1.0
C16 B:PJF301 4.0 53.9 1.0
CG B:ARG78 4.0 52.7 1.0
C20 B:PJF301 4.0 44.2 1.0
CD1 A:PHE105 4.1 46.9 1.0
N A:PHE105 4.2 41.3 1.0
CG B:LEU79 4.3 47.4 1.0
CG A:PHE105 4.4 47.2 1.0
C15 B:PJF301 4.5 48.2 1.0
N B:LEU79 4.6 50.1 1.0
CG B:GLU82 4.6 56.2 1.0
CA B:LEU79 4.6 47.5 1.0
NH1 B:ARG78 4.6 53.2 1.0
O A:LEU104 4.6 45.5 1.0
C A:LEU104 4.6 44.0 1.0
O A:ALA101 4.7 41.8 1.0
C B:ARG78 4.7 53.6 1.0
O B:ARG78 4.8 51.0 1.0
CB B:ARG78 4.8 56.3 1.0
CZ B:ARG78 4.8 61.3 1.0

Chlorine binding site 3 out of 7 in 7uvr

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Chlorine binding site 3 out of 7 in the Crystal Structure of Human Clpp Protease in Complex with Tr-65


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 Human Clpp Protease in Complex with Tr-65 within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cl301

b:62.0
occ:1.00
 CL1 C:PJF301 0.0 62.0 1.0
C18 C:PJF301 1.7 55.3 1.0
C17 C:PJF301 2.7 51.5 1.0
C19 C:PJF301 2.7 50.7 1.0
CB B:PHE105 3.4 44.6 1.0
CA B:PHE105 3.6 45.1 1.0
CG C:ARG78 3.9 51.8 1.0
CD1 B:PHE105 3.9 41.8 1.0
N B:PHE105 4.0 41.7 1.0
CD2 C:LEU79 4.0 54.1 1.0
C16 C:PJF301 4.0 48.4 1.0
C20 C:PJF301 4.0 55.6 1.0
CG B:PHE105 4.1 49.0 1.0
C15 C:PJF301 4.5 52.6 1.0
CD1 C:ILE75 4.6 40.7 1.0
N C:LEU79 4.6 46.4 1.0
O C:ARG78 4.6 50.0 1.0
CG C:LEU79 4.6 54.2 1.0
C C:ARG78 4.6 50.5 1.0
O B:ALA101 4.6 45.2 1.0
CB C:ARG78 4.7 57.9 1.0
CA C:LEU79 4.7 45.2 1.0
C B:LEU104 4.7 43.3 1.0
CZ C:ARG78 4.8 57.1 1.0
NE C:ARG78 4.9 55.2 1.0
O C:ILE75 4.9 50.5 1.0
C B:PHE105 5.0 45.1 1.0

Chlorine binding site 4 out of 7 in 7uvr

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Chlorine binding site 4 out of 7 in the Crystal Structure of Human Clpp Protease in Complex with Tr-65


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 Human Clpp Protease in Complex with Tr-65 within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Cl301

b:59.0
occ:1.00
 CL1 D:PJF301 0.0 59.0 1.0
C18 D:PJF301 1.7 52.9 1.0
C19 D:PJF301 2.7 47.8 1.0
C17 D:PJF301 2.7 54.4 1.0
CD2 D:LEU79 3.4 46.5 1.0
CB C:PHE105 3.7 45.0 1.0
CA C:PHE105 3.7 45.1 1.0
N C:PHE105 4.0 42.3 1.0
C20 D:PJF301 4.0 47.0 1.0
C16 D:PJF301 4.0 49.8 1.0
CG D:ARG78 4.1 48.2 1.0
CD1 C:PHE105 4.3 47.2 1.0
C15 D:PJF301 4.5 43.7 1.0
NH1 D:ARG78 4.5 50.5 1.0
CG C:PHE105 4.5 45.2 1.0
O C:ALA101 4.5 50.7 1.0
O D:ARG78 4.5 51.7 1.0
CG D:LEU79 4.5 44.9 1.0
N D:LEU79 4.6 44.0 1.0
CA D:LEU79 4.6 44.0 1.0
C D:ARG78 4.6 45.8 1.0
C C:LEU104 4.6 43.1 1.0
CZ D:ARG78 4.7 61.8 1.0
CG D:GLU82 4.7 54.1 1.0
O D:ILE75 4.9 43.4 1.0
CB D:ARG78 4.9 46.0 1.0
CG1 D:ILE75 5.0 45.5 1.0
O C:LEU104 5.0 45.8 1.0
NE D:ARG78 5.0 56.5 1.0

Chlorine binding site 5 out of 7 in 7uvr

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Chlorine binding site 5 out of 7 in the Crystal Structure of Human Clpp Protease in Complex with Tr-65


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 Human Clpp Protease in Complex with Tr-65 within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Cl301

b:60.3
occ:1.00
 CL1 E:PJF301 0.0 60.3 1.0
C18 E:PJF301 1.7 48.8 1.0
C17 E:PJF301 2.7 46.4 1.0
C19 E:PJF301 2.7 45.1 1.0
CG E:ARG78 3.8 38.9 1.0
CB D:PHE105 3.9 36.5 1.0
CA D:PHE105 3.9 42.3 1.0
C16 E:PJF301 4.0 43.5 1.0
C20 E:PJF301 4.0 47.1 1.0
CD2 E:LEU79 4.1 44.2 1.0
CD1 D:PHE105 4.2 42.3 1.0
N D:PHE105 4.3 46.0 1.0
CG E:LEU79 4.3 45.8 1.0
CA E:LEU79 4.3 41.3 1.0
N E:LEU79 4.4 45.6 1.0
NH1 E:ARG78 4.4 45.1 1.0
O D:ALA101 4.4 53.2 1.0
C E:ARG78 4.5 40.1 1.0
C15 E:PJF301 4.5 43.3 1.0
O E:ARG78 4.5 43.2 1.0
CG D:PHE105 4.5 49.1 1.0
CZ E:ARG78 4.6 46.1 1.0
CB E:ARG78 4.7 47.6 1.0
NE E:ARG78 4.8 42.5 1.0
CD1 E:ILE75 4.8 46.6 1.0
C D:LEU104 4.8 47.6 1.0
CB E:LEU79 4.8 42.6 1.0
CD E:ARG78 4.8 42.3 1.0
O E:ILE75 5.0 44.0 1.0
OE1 E:GLU82 5.0 52.2 1.0

Chlorine binding site 6 out of 7 in 7uvr

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Chlorine binding site 6 out of 7 in the Crystal Structure of Human Clpp Protease in Complex with Tr-65


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 Human Clpp Protease in Complex with Tr-65 within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Cl301

b:59.2
occ:1.00
 CL1 F:PJF301 0.0 59.2 1.0
C18 F:PJF301 1.7 46.0 1.0
C17 F:PJF301 2.7 45.0 1.0
C19 F:PJF301 2.7 47.3 1.0
CD2 F:LEU79 3.4 49.4 1.0
CB E:PHE105 3.6 43.1 1.0
CA E:PHE105 3.7 43.6 1.0
CD1 E:PHE105 3.8 46.1 1.0
CG F:ARG78 3.8 47.3 1.0
C16 F:PJF301 4.0 50.9 1.0
C20 F:PJF301 4.0 44.1 1.0
N E:PHE105 4.0 43.1 1.0
CG E:PHE105 4.2 44.8 1.0
CG F:GLU82 4.5 48.0 1.0
N F:LEU79 4.5 45.9 1.0
CG F:LEU79 4.5 47.6 1.0
C15 F:PJF301 4.5 48.2 1.0
O E:ALA101 4.5 43.6 1.0
CA F:LEU79 4.5 44.1 1.0
C F:ARG78 4.6 44.2 1.0
CB F:ARG78 4.6 43.6 1.0
O F:ARG78 4.7 47.8 1.0
NH1 F:ARG78 4.7 46.1 1.0
C E:LEU104 4.8 44.4 1.0
CD F:ARG78 4.8 50.2 1.0
CG1 F:ILE75 4.9 35.5 1.0
CE1 E:PHE105 4.9 46.0 1.0

Chlorine binding site 7 out of 7 in 7uvr

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Chlorine binding site 7 out of 7 in the Crystal Structure of Human Clpp Protease in Complex with Tr-65


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 Human Clpp Protease in Complex with Tr-65 within 5.0Å range:
probe atom residue distance (Å) B Occ
G:Cl301

b:62.6
occ:1.00
 CL1 G:PJF301 0.0 62.6 1.0
C18 G:PJF301 1.7 43.8 1.0
C17 G:PJF301 2.7 43.4 1.0
C19 G:PJF301 2.7 35.5 1.0
CD2 G:LEU79 3.5 34.9 1.0
CB F:PHE105 3.8 39.9 1.0
CA F:PHE105 3.9 39.4 1.0
CG G:ARG78 3.9 44.2 1.0
C16 G:PJF301 4.0 43.0 1.0
C20 G:PJF301 4.0 37.7 1.0
NH1 G:ARG78 4.1 40.6 1.0
CG G:GLU82 4.2 48.2 1.0
CD1 F:PHE105 4.2 35.8 1.0
N F:PHE105 4.3 36.2 1.0
O G:ARG78 4.4 48.6 1.0
CG F:PHE105 4.5 38.3 1.0
C15 G:PJF301 4.5 36.7 1.0
CZ G:ARG78 4.5 46.0 1.0
CA G:LEU79 4.6 42.2 1.0
C G:ARG78 4.6 44.2 1.0
N G:LEU79 4.6 46.3 1.0
CG G:LEU79 4.6 32.2 1.0
O F:ALA101 4.7 40.7 1.0
C F:LEU104 4.8 37.3 1.0
CB G:ARG78 4.8 50.4 1.0
O F:LEU104 4.8 48.7 1.0
CD G:ARG78 4.9 41.2 1.0
NE G:ARG78 4.9 42.9 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: Tue Jul 30 05:11:37 2024

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