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Chlorine in PDB 7uvu: Crystal Structure of Human Clpp Protease in Complex with Tr-107

Enzymatic activity of Crystal Structure of Human Clpp Protease in Complex with Tr-107

All present enzymatic activity of Crystal Structure of Human Clpp Protease in Complex with Tr-107:
3.4.21.92;

Protein crystallography data

The structure of Crystal Structure of Human Clpp Protease in Complex with Tr-107, PDB code: 7uvu 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) 48.47 / 3.24
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 142.147, 152.662, 104.342, 90, 118.01, 90
R / Rfree (%) 19 / 26.1

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Human Clpp Protease in Complex with Tr-107 (pdb code 7uvu). 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-107, PDB code: 7uvu:
Jump to Chlorine binding site number: 1; 2; 3; 4; 5; 6; 7;

Chlorine binding site 1 out of 7 in 7uvu

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Chlorine binding site 1 out of 7 in the Crystal Structure of Human Clpp Protease in Complex with Tr-107


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-107 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl301

b:61.8
occ:1.00
 CL21 A:OY9301 0.0 61.8 1.0
C20 A:OY9301 1.9 53.3 1.0
C19 A:OY9301 2.8 48.5 1.0
C22 A:OY9301 2.9 55.7 1.0
CG A:ARG78 3.7 53.1 1.0
CD1 G:PHE105 3.7 45.1 1.0
CB G:PHE105 3.7 44.8 1.0
CA G:PHE105 3.8 44.8 1.0
CD2 A:LEU79 3.8 44.9 1.0
C18 A:OY9301 4.1 54.2 1.0
CG G:PHE105 4.2 44.8 1.0
C23 A:OY9301 4.2 51.4 1.0
N G:PHE105 4.2 41.8 1.0
CG A:LEU79 4.4 43.5 1.0
CB A:ARG78 4.5 53.3 1.0
O G:ALA101 4.5 42.7 1.0
CG1 A:ILE75 4.6 39.7 1.0
C17 A:OY9301 4.7 50.5 1.0
N A:LEU79 4.7 48.5 1.0
C A:ARG78 4.7 48.3 1.0
NH1 A:ARG78 4.7 68.9 1.0
CZ A:ARG78 4.7 67.0 1.0
CE1 G:PHE105 4.8 46.8 1.0
O A:ARG78 4.8 48.3 1.0
NE A:ARG78 4.8 65.9 1.0
CD A:ARG78 4.8 59.4 1.0
C G:LEU104 4.8 40.4 1.0
CA A:LEU79 4.8 46.5 1.0
CD1 A:ILE75 5.0 43.3 1.0
O A:ILE75 5.0 42.0 1.0

Chlorine binding site 2 out of 7 in 7uvu

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Chlorine binding site 2 out of 7 in the Crystal Structure of Human Clpp Protease in Complex with Tr-107


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-107 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl301

b:55.5
occ:1.00
 CL21 B:OY9301 0.0 55.5 1.0
C20 B:OY9301 1.9 56.1 1.0
C19 B:OY9301 2.9 51.2 1.0
C22 B:OY9301 2.9 53.8 1.0
CD2 B:LEU79 3.5 44.9 1.0
CG B:ARG78 3.6 46.0 1.0
CB A:PHE105 3.6 42.7 1.0
CD1 A:PHE105 3.8 45.6 1.0
CA A:PHE105 4.0 43.8 1.0
CG A:PHE105 4.2 45.9 1.0
C18 B:OY9301 4.2 50.6 1.0
C23 B:OY9301 4.2 51.4 1.0
CG B:LEU79 4.3 45.6 1.0
N B:LEU79 4.4 45.1 1.0
CB B:ARG78 4.4 46.5 1.0
N A:PHE105 4.5 42.4 1.0
CA B:LEU79 4.5 45.7 1.0
CZ B:ARG78 4.5 49.4 1.0
NE B:ARG78 4.5 48.9 1.0
O A:ALA101 4.5 44.1 1.0
C B:ARG78 4.6 45.4 1.0
C17 B:OY9301 4.7 50.3 1.0
CD B:ARG78 4.7 47.0 1.0
NH1 B:ARG78 4.7 51.7 1.0
O B:ILE75 4.8 42.9 1.0
O B:ARG78 4.8 46.8 1.0
CG1 B:ILE75 4.9 38.7 1.0
NH2 B:ARG78 4.9 50.5 1.0
CE1 A:PHE105 4.9 43.2 1.0
CG B:GLU82 5.0 47.4 1.0

Chlorine binding site 3 out of 7 in 7uvu

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Chlorine binding site 3 out of 7 in the Crystal Structure of Human Clpp Protease in Complex with Tr-107


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-107 within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cl301

b:57.0
occ:1.00
 CL21 C:OY9301 0.0 57.0 1.0
C20 C:OY9301 1.9 55.3 1.0
C22 C:OY9301 2.8 59.2 1.0
C19 C:OY9301 2.9 49.4 1.0
CB B:PHE105 3.6 46.4 1.0
CG C:ARG78 3.7 53.9 1.0
CA B:PHE105 3.8 46.1 1.0
CD1 B:PHE105 3.9 46.8 1.0
N B:PHE105 4.2 45.0 1.0
C23 C:OY9301 4.2 55.5 1.0
CG B:PHE105 4.2 48.4 1.0
C18 C:OY9301 4.2 51.5 1.0
CD2 C:LEU79 4.3 45.7 1.0
NH1 C:ARG78 4.3 59.0 1.0
N C:LEU79 4.5 54.6 1.0
O B:ALA101 4.5 45.2 1.0
C C:ARG78 4.5 54.8 1.0
CB C:ARG78 4.6 55.6 1.0
O C:ARG78 4.6 54.1 1.0
CA C:LEU79 4.6 48.4 1.0
CG C:LEU79 4.7 52.0 1.0
C17 C:OY9301 4.7 51.7 1.0
CZ C:ARG78 4.7 65.8 1.0
CG C:GLU82 4.8 56.1 1.0
C B:LEU104 4.8 47.6 1.0
CG1 C:ILE75 4.9 39.1 1.0
O C:ILE75 4.9 52.7 1.0
CD C:ARG78 4.9 59.4 1.0
NE C:ARG78 5.0 65.7 1.0

Chlorine binding site 4 out of 7 in 7uvu

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Chlorine binding site 4 out of 7 in the Crystal Structure of Human Clpp Protease in Complex with Tr-107


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-107 within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Cl301

b:63.0
occ:1.00
 CL21 D:OY9301 0.0 63.0 1.0
C20 D:OY9301 1.9 55.6 1.0
C22 D:OY9301 2.9 52.5 1.0
C19 D:OY9301 2.9 51.6 1.0
CD2 D:LEU79 3.5 44.2 1.0
CB C:PHE105 3.8 50.8 1.0
CG D:ARG78 3.8 41.5 1.0
CA C:PHE105 3.8 44.9 1.0
CD1 C:PHE105 3.9 43.3 1.0
N C:PHE105 4.2 36.3 1.0
C23 D:OY9301 4.2 48.2 1.0
C18 D:OY9301 4.2 48.7 1.0
CG C:PHE105 4.3 49.7 1.0
CG D:LEU79 4.4 48.2 1.0
NE D:ARG78 4.4 48.7 1.0
N D:LEU79 4.5 47.4 1.0
CZ D:ARG78 4.5 52.0 1.0
CA D:LEU79 4.6 47.1 1.0
O C:ALA101 4.6 42.0 1.0
C D:ARG78 4.6 42.9 1.0
O D:ARG78 4.7 42.8 1.0
CB D:ARG78 4.7 40.6 1.0
C17 D:OY9301 4.7 46.9 1.0
CD D:ARG78 4.7 50.3 1.0
NH2 D:ARG78 4.8 49.2 1.0
CG D:GLU82 4.8 47.6 1.0
C C:LEU104 4.9 40.1 1.0
CG1 D:ILE75 5.0 38.9 1.0
NH1 D:ARG78 5.0 51.4 1.0

Chlorine binding site 5 out of 7 in 7uvu

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Chlorine binding site 5 out of 7 in the Crystal Structure of Human Clpp Protease in Complex with Tr-107


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-107 within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Cl301

b:57.4
occ:1.00
 CL21 E:OY9301 0.0 57.4 1.0
C20 E:OY9301 1.9 48.5 1.0
C19 E:OY9301 2.8 43.9 1.0
C22 E:OY9301 2.9 43.8 1.0
CG E:ARG78 3.5 41.7 1.0
CB D:PHE105 3.8 46.8 1.0
CA D:PHE105 4.0 43.7 1.0
CD1 D:PHE105 4.0 40.8 1.0
CD2 E:LEU79 4.0 39.5 1.0
C18 E:OY9301 4.2 43.4 1.0
C23 E:OY9301 4.2 42.8 1.0
C E:ARG78 4.4 47.0 1.0
O E:ARG78 4.4 49.1 1.0
N E:LEU79 4.4 44.8 1.0
CB E:ARG78 4.4 48.0 1.0
NH1 E:ARG78 4.4 46.8 1.0
CG D:PHE105 4.4 47.1 1.0
N D:PHE105 4.4 44.7 1.0
CZ E:ARG78 4.5 49.5 1.0
CA E:LEU79 4.5 44.9 1.0
NE E:ARG78 4.5 53.4 1.0
CD E:ARG78 4.5 50.9 1.0
CG E:GLU82 4.6 50.5 1.0
CG E:LEU79 4.6 43.8 1.0
C17 E:OY9301 4.7 46.8 1.0
O D:ALA101 4.8 42.0 1.0
C D:LEU104 4.8 44.8 1.0
O D:LEU104 4.9 41.0 1.0

Chlorine binding site 6 out of 7 in 7uvu

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Chlorine binding site 6 out of 7 in the Crystal Structure of Human Clpp Protease in Complex with Tr-107


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-107 within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Cl301

b:54.8
occ:1.00
 CL21 F:OY9301 0.0 54.8 1.0
C20 F:OY9301 1.9 49.3 1.0
C19 F:OY9301 2.8 45.0 1.0
C22 F:OY9301 2.9 46.0 1.0
CD2 F:LEU79 3.4 49.6 1.0
CB E:PHE105 3.8 48.0 1.0
CG F:ARG78 3.8 41.5 1.0
CA E:PHE105 3.8 44.1 1.0
CD1 E:PHE105 3.8 46.5 1.0
C18 F:OY9301 4.1 49.3 1.0
C23 F:OY9301 4.2 47.2 1.0
CG F:LEU79 4.2 49.5 1.0
N E:PHE105 4.3 39.9 1.0
CG E:PHE105 4.3 48.2 1.0
O E:ALA101 4.4 42.7 1.0
CZ F:ARG78 4.5 47.7 1.0
N F:LEU79 4.5 44.5 1.0
CB F:ARG78 4.6 44.9 1.0
CA F:LEU79 4.6 48.0 1.0
C F:ARG78 4.6 41.3 1.0
CG F:GLU82 4.6 45.3 1.0
C17 F:OY9301 4.6 51.5 1.0
O F:ARG78 4.6 43.1 1.0
NH1 F:ARG78 4.7 60.8 1.0
NE F:ARG78 4.7 49.4 1.0
NH2 F:ARG78 4.8 43.3 1.0
CD F:ARG78 4.9 47.9 1.0
C E:LEU104 4.9 40.1 1.0
CE1 E:PHE105 5.0 51.2 1.0

Chlorine binding site 7 out of 7 in 7uvu

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Chlorine binding site 7 out of 7 in the Crystal Structure of Human Clpp Protease in Complex with Tr-107


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-107 within 5.0Å range:
probe atom residue distance (Å) B Occ
G:Cl301

b:62.0
occ:1.00
 CL21 G:OY9301 0.0 62.0 1.0
C20 G:OY9301 2.0 51.8 1.0
C22 G:OY9301 2.9 51.3 1.0
C19 G:OY9301 2.9 44.6 1.0
CG G:ARG78 3.4 48.9 1.0
CD2 G:LEU79 3.6 45.4 1.0
CB F:PHE105 3.9 45.3 1.0
CA F:PHE105 4.1 38.7 1.0
CD1 F:PHE105 4.2 40.9 1.0
NE G:ARG78 4.2 56.3 1.0
C23 G:OY9301 4.2 46.9 1.0
C18 G:OY9301 4.3 40.2 1.0
CB G:ARG78 4.3 52.4 1.0
C G:ARG78 4.3 52.1 1.0
N G:LEU79 4.3 48.7 1.0
O G:ARG78 4.3 58.1 1.0
CA G:LEU79 4.4 47.7 1.0
CD G:ARG78 4.5 53.9 1.0
CZ G:ARG78 4.5 55.5 1.0
CG F:PHE105 4.5 42.5 1.0
N F:PHE105 4.5 33.1 1.0
CG G:LEU79 4.6 44.0 1.0
CG G:GLU82 4.6 47.6 1.0
NH2 G:ARG78 4.7 55.2 1.0
C17 G:OY9301 4.8 42.3 1.0
O F:ALA101 4.9 42.6 1.0
O G:ILE75 4.9 44.8 1.0
CA G:ARG78 4.9 48.6 1.0
CG1 G:ILE75 5.0 37.3 1.0
CB G:LEU79 5.0 47.0 1.0
NH1 G:ARG78 5.0 56.0 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: Tue Jul 30 05:11:37 2024

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