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Chlorine in PDB 7uvn: Crystal Structure of Human Clpp Protease in Complex with Tr-57

Enzymatic activity of Crystal Structure of Human Clpp Protease in Complex with Tr-57

All present enzymatic activity of Crystal Structure of Human Clpp Protease in Complex with Tr-57:
3.4.21.92;

Protein crystallography data

The structure of Crystal Structure of Human Clpp Protease in Complex with Tr-57, PDB code: 7uvn 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) 49.25 / 3.11
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 142.098, 153.04, 104.696, 90, 117.92, 90
R / Rfree (%) 22.9 / 28.3

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Human Clpp Protease in Complex with Tr-57 (pdb code 7uvn). 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-57, PDB code: 7uvn:
Jump to Chlorine binding site number: 1; 2; 3; 4; 5; 6; 7;

Chlorine binding site 1 out of 7 in 7uvn

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Chlorine binding site 1 out of 7 in the Crystal Structure of Human Clpp Protease in Complex with Tr-57


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-57 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl301

b:70.7
occ:1.00
 CL01 A:P3O301 0.0 70.7 1.0
C02 A:P3O301 1.8 56.6 1.0
C03 A:P3O301 2.8 52.1 1.0
C30 A:P3O301 2.8 53.1 1.0
CG A:ARG78 3.4 54.5 1.0
CB G:PHE105 3.5 46.1 1.0
CD1 G:PHE105 3.5 50.0 1.0
CD2 A:LEU79 3.6 45.9 1.0
CA G:PHE105 3.8 46.4 1.0
CG G:PHE105 4.0 52.0 1.0
C04 A:P3O301 4.0 51.6 1.0
C29 A:P3O301 4.1 52.3 1.0
O A:ARG78 4.1 52.7 1.0
C A:ARG78 4.2 54.8 1.0
NH1 A:ARG78 4.2 52.1 1.0
CB A:ARG78 4.2 54.0 1.0
N A:LEU79 4.3 59.6 1.0
N G:PHE105 4.4 48.6 1.0
CZ A:ARG78 4.4 58.1 1.0
CA A:LEU79 4.4 54.7 1.0
NE A:ARG78 4.5 60.4 1.0
CD A:ARG78 4.5 56.9 1.0
C05 A:P3O301 4.6 50.1 1.0
CG A:LEU79 4.6 45.1 1.0
CE1 G:PHE105 4.7 49.7 1.0
O G:ALA101 4.7 42.1 1.0
CG A:GLU82 4.8 57.4 1.0
O A:ILE75 4.8 45.2 1.0
CG1 A:ILE75 4.9 38.4 1.0
CA A:ARG78 4.9 57.8 1.0
C G:LEU104 5.0 47.4 1.0

Chlorine binding site 2 out of 7 in 7uvn

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Chlorine binding site 2 out of 7 in the Crystal Structure of Human Clpp Protease in Complex with Tr-57


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-57 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl301

b:72.0
occ:1.00
 CL01 B:P3O301 0.0 72.0 1.0
C02 B:P3O301 1.8 55.5 1.0
C03 B:P3O301 2.8 54.9 1.0
C30 B:P3O301 2.8 52.9 1.0
CG B:ARG78 3.3 48.2 1.0
CD2 B:LEU79 3.4 43.9 1.0
CD1 A:PHE105 3.7 45.3 1.0
CB A:PHE105 3.7 45.7 1.0
CA A:PHE105 4.0 47.5 1.0
C04 B:P3O301 4.0 52.3 1.0
C29 B:P3O301 4.1 56.6 1.0
NH1 B:ARG78 4.1 58.9 1.0
CG A:PHE105 4.1 47.6 1.0
CB B:ARG78 4.2 49.9 1.0
O B:ARG78 4.3 52.5 1.0
C B:ARG78 4.3 52.3 1.0
N B:LEU79 4.4 50.9 1.0
CZ B:ARG78 4.4 65.2 1.0
CD B:ARG78 4.5 57.1 1.0
C05 B:P3O301 4.6 51.4 1.0
N A:PHE105 4.6 49.2 1.0
NE B:ARG78 4.6 63.4 1.0
CG B:LEU79 4.7 46.8 1.0
CA B:LEU79 4.7 49.5 1.0
CE1 A:PHE105 4.7 51.4 1.0
CG B:GLU82 4.8 47.0 1.0
O A:ALA101 4.8 41.7 1.0
O B:ILE75 4.8 49.0 1.0
CA B:ARG78 4.9 54.0 1.0
CG1 B:ILE75 5.0 31.9 1.0
OG A:SER108 5.0 50.6 1.0

Chlorine binding site 3 out of 7 in 7uvn

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Chlorine binding site 3 out of 7 in the Crystal Structure of Human Clpp Protease in Complex with Tr-57


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-57 within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cl301

b:70.5
occ:1.00
 CL01 C:P3O301 0.0 70.5 1.0
C02 C:P3O301 1.8 54.2 1.0
C03 C:P3O301 2.8 51.7 1.0
C30 C:P3O301 2.8 46.1 1.0
CG C:ARG78 3.4 52.1 1.0
CD2 C:LEU79 3.5 46.8 1.0
CD1 B:PHE105 3.7 44.5 1.0
CB B:PHE105 3.8 42.3 1.0
C04 C:P3O301 4.0 49.0 1.0
CA B:PHE105 4.1 38.5 1.0
C29 C:P3O301 4.1 45.5 1.0
O C:ARG78 4.2 56.5 1.0
CG B:PHE105 4.2 46.4 1.0
CZ C:ARG78 4.2 59.0 1.0
C C:ARG78 4.2 55.0 1.0
NH1 C:ARG78 4.3 63.1 1.0
N C:LEU79 4.3 54.0 1.0
CB C:ARG78 4.3 54.2 1.0
NE C:ARG78 4.3 52.7 1.0
CA C:LEU79 4.4 52.3 1.0
CD C:ARG78 4.4 51.8 1.0
C05 C:P3O301 4.6 44.6 1.0
CD1 C:ILE75 4.6 36.9 1.0
CG C:LEU79 4.6 50.4 1.0
N B:PHE105 4.6 37.5 1.0
NH2 C:ARG78 4.8 60.4 1.0
O B:ALA101 4.8 41.2 1.0
CE1 B:PHE105 4.8 46.7 1.0
O C:ILE75 4.8 51.1 1.0
CA C:ARG78 4.9 56.5 1.0

Chlorine binding site 4 out of 7 in 7uvn

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Chlorine binding site 4 out of 7 in the Crystal Structure of Human Clpp Protease in Complex with Tr-57


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-57 within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Cl301

b:69.7
occ:1.00
 CL01 D:P3O301 0.0 69.7 1.0
C02 D:P3O301 1.8 59.4 1.0
C03 D:P3O301 2.8 57.6 1.0
C30 D:P3O301 2.8 58.4 1.0
CB C:PHE105 3.5 50.1 1.0
CD2 D:LEU79 3.6 44.8 1.0
CG D:ARG78 3.7 54.4 1.0
CA C:PHE105 3.7 51.9 1.0
CD1 C:PHE105 3.8 49.5 1.0
C04 D:P3O301 4.0 53.3 1.0
C29 D:P3O301 4.1 56.3 1.0
CG C:PHE105 4.1 47.9 1.0
N C:PHE105 4.2 49.7 1.0
O D:ARG78 4.4 53.8 1.0
CB D:ARG78 4.5 48.6 1.0
C D:ARG78 4.6 54.7 1.0
C05 D:P3O301 4.6 52.1 1.0
CG D:LEU79 4.6 51.9 1.0
O C:ALA101 4.6 43.6 1.0
N D:LEU79 4.7 53.6 1.0
CD D:ARG78 4.8 57.7 1.0
CA D:LEU79 4.8 48.4 1.0
NE D:ARG78 4.8 61.1 1.0
CG D:GLU82 4.8 50.8 1.0
CG1 D:ILE75 4.9 37.9 1.0
CE1 C:PHE105 4.9 49.8 1.0
O D:ILE75 5.0 51.5 1.0
C C:LEU104 5.0 51.5 1.0

Chlorine binding site 5 out of 7 in 7uvn

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Chlorine binding site 5 out of 7 in the Crystal Structure of Human Clpp Protease in Complex with Tr-57


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-57 within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Cl301

b:71.1
occ:1.00
 CL01 E:P3O301 0.0 71.1 1.0
C02 E:P3O301 1.8 54.7 1.0
C03 E:P3O301 2.8 51.9 1.0
C30 E:P3O301 2.8 50.2 1.0
CD2 E:LEU79 3.5 44.0 1.0
CB D:PHE105 3.5 44.2 1.0
CG E:ARG78 3.5 54.2 1.0
CA D:PHE105 3.8 50.9 1.0
CD1 D:PHE105 3.9 48.2 1.0
C04 E:P3O301 4.0 49.7 1.0
C29 E:P3O301 4.1 53.3 1.0
CG D:PHE105 4.1 50.6 1.0
NH1 E:ARG78 4.3 60.8 1.0
CB E:ARG78 4.4 55.9 1.0
N D:PHE105 4.4 51.2 1.0
CG E:LEU79 4.4 51.0 1.0
CZ E:ARG78 4.4 56.8 1.0
N E:LEU79 4.4 55.1 1.0
C E:ARG78 4.4 54.5 1.0
O E:ARG78 4.4 56.4 1.0
NE E:ARG78 4.5 51.2 1.0
CD E:ARG78 4.5 48.7 1.0
CA E:LEU79 4.5 53.7 1.0
C05 E:P3O301 4.6 49.3 1.0
O D:ALA101 4.6 47.8 1.0
OG D:SER108 4.8 50.7 1.0
O E:ILE75 4.8 50.2 1.0
CD1 E:ILE75 4.9 46.8 1.0

Chlorine binding site 6 out of 7 in 7uvn

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Chlorine binding site 6 out of 7 in the Crystal Structure of Human Clpp Protease in Complex with Tr-57


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-57 within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Cl301

b:73.4
occ:1.00
 CL01 F:P3O301 0.0 73.4 1.0
C02 F:P3O301 1.8 66.9 1.0
C03 F:P3O301 2.8 61.9 1.0
C30 F:P3O301 2.8 65.0 1.0
CB E:PHE105 3.4 50.4 1.0
CG F:ARG78 3.5 63.4 1.0
CD2 F:LEU79 3.6 62.5 1.0
CA E:PHE105 3.8 50.0 1.0
CD1 E:PHE105 3.9 54.6 1.0
C04 F:P3O301 4.0 59.8 1.0
C29 F:P3O301 4.1 61.7 1.0
CG E:PHE105 4.1 53.1 1.0
O F:ARG78 4.2 58.3 1.0
C F:ARG78 4.3 60.8 1.0
N E:PHE105 4.3 52.9 1.0
CB F:ARG78 4.3 61.6 1.0
N F:LEU79 4.3 58.8 1.0
CA F:LEU79 4.4 53.4 1.0
CG F:LEU79 4.5 65.7 1.0
O E:ALA101 4.5 48.7 1.0
C05 F:P3O301 4.6 63.6 1.0
CD F:ARG78 4.6 67.9 1.0
NE F:ARG78 4.6 73.5 1.0
CD1 F:ILE75 4.7 54.0 1.0
CZ F:ARG78 4.8 76.9 1.0
O F:ILE75 4.8 59.8 1.0
CG F:GLU82 4.8 59.3 1.0
NH1 F:ARG78 4.9 76.9 1.0
CA F:ARG78 5.0 62.2 1.0
C E:LEU104 5.0 56.3 1.0

Chlorine binding site 7 out of 7 in 7uvn

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Chlorine binding site 7 out of 7 in the Crystal Structure of Human Clpp Protease in Complex with Tr-57


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-57 within 5.0Å range:
probe atom residue distance (Å) B Occ
G:Cl301

b:69.5
occ:1.00
 CL01 G:P3O301 0.0 69.5 1.0
C02 G:P3O301 1.8 59.0 1.0
C03 G:P3O301 2.8 53.2 1.0
C30 G:P3O301 2.8 56.7 1.0
CD2 G:LEU79 3.5 44.9 1.0
CG G:ARG78 3.6 48.7 1.0
CB F:PHE105 3.6 51.7 1.0
CA F:PHE105 3.9 45.8 1.0
CD1 F:PHE105 4.0 53.2 1.0
C04 G:P3O301 4.0 52.2 1.0
C29 G:P3O301 4.1 55.8 1.0
CG F:PHE105 4.3 52.8 1.0
N G:LEU79 4.4 46.0 1.0
N F:PHE105 4.4 43.9 1.0
CG G:LEU79 4.4 45.8 1.0
CB G:ARG78 4.4 44.4 1.0
C G:ARG78 4.4 45.4 1.0
O G:ARG78 4.4 45.0 1.0
CA G:LEU79 4.5 45.0 1.0
C05 G:P3O301 4.6 47.2 1.0
O F:ALA101 4.6 46.7 1.0
NH1 G:ARG78 4.7 54.2 1.0
CZ G:ARG78 4.8 65.6 1.0
CD G:ARG78 4.8 60.9 1.0
O G:ILE75 4.8 47.1 1.0
NE G:ARG78 4.8 64.8 1.0
CG1 G:ILE75 4.9 42.7 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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