Bromine in PDB 8hgk: Crystal Structure of Human Clpp in Complex with ZK53

Enzymatic activity of Crystal Structure of Human Clpp in Complex with ZK53

All present enzymatic activity of Crystal Structure of Human Clpp in Complex with ZK53:
3.4.21.92;

Protein crystallography data

The structure of Crystal Structure of Human Clpp in Complex with ZK53, PDB code: 8hgk was solved by C.-G.Yang, J.H.Gan, L.-L.Zhou, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.53 / 1.90
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 120.31, 97, 123.84, 90, 93.98, 90
R / Rfree (%) 18.6 / 22.1

Other elements in 8hgk:

The structure of Crystal Structure of Human Clpp in Complex with ZK53 also contains other interesting chemical elements:

Fluorine (F) 28 atoms
Magnesium (Mg) 5 atoms

Bromine Binding Sites:

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 14;

Binding sites:

The binding sites of Bromine atom in the Crystal Structure of Human Clpp in Complex with ZK53 (pdb code 8hgk). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total 14 binding sites of Bromine where determined in the Crystal Structure of Human Clpp in Complex with ZK53, PDB code: 8hgk:
Jump to Bromine binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Bromine binding site 1 out of 14 in 8hgk

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Bromine binding site 1 out of 14 in the Crystal Structure of Human Clpp in Complex with ZK53


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 in Complex with ZK53 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Br301

b:162.7
occ:1.00
BR1 A:ZLL301 0.0 162.7 1.0
C2 A:ZLL301 1.9 121.7 1.0
C3 A:ZLL301 2.9 99.7 1.0
C7 A:ZLL301 2.9 112.3 1.0
CD2 A:LEU79 3.6 49.7 1.0
CA G:PHE105 3.7 32.1 1.0
CB G:PHE105 3.9 33.3 1.0
CD1 G:PHE105 4.0 35.3 1.0
CG A:GLU82 4.2 46.1 1.0
N G:PHE105 4.2 29.9 1.0
CG A:ARG78 4.2 46.7 1.0
C4 A:ZLL301 4.2 93.1 1.0
C6 A:ZLL301 4.2 104.5 1.0
OG G:SER108 4.3 44.2 1.0
NH1 A:ARG78 4.4 54.5 1.0
CG G:PHE105 4.4 34.4 1.0
CG A:LEU79 4.6 44.4 1.0
CZ A:ARG78 4.6 55.1 1.0
CA A:LEU79 4.7 33.7 1.0
C G:LEU104 4.7 27.4 1.0
O G:LEU104 4.7 30.9 1.0
O A:ARG78 4.7 36.9 1.0
C5 A:ZLL301 4.8 91.9 1.0
N A:LEU79 4.8 27.2 1.0
C A:ARG78 4.9 33.9 1.0
NE A:ARG78 4.9 54.9 1.0
C G:PHE105 5.0 31.6 1.0

Bromine binding site 2 out of 14 in 8hgk

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Bromine binding site 2 out of 14 in the Crystal Structure of Human Clpp in Complex with ZK53


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 in Complex with ZK53 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Br302

b:155.5
occ:1.00
BR1 A:ZLL302 0.0 155.5 1.0
C2 A:ZLL302 1.9 115.2 1.0
C3 A:ZLL302 2.9 94.3 1.0
C7 A:ZLL302 2.9 111.2 1.0
CD2 B:LEU79 3.6 50.0 1.0
CA A:PHE105 3.9 31.3 1.0
CG B:GLU82 4.0 49.9 1.0
CD1 A:PHE105 4.1 33.6 1.0
CB A:PHE105 4.1 32.9 1.0
C4 A:ZLL302 4.2 99.8 1.0
CG B:ARG78 4.2 41.1 1.0
NH1 B:ARG78 4.2 56.5 1.0
C6 A:ZLL302 4.2 111.7 1.0
OG A:SER108 4.3 47.7 1.0
N A:PHE105 4.4 30.4 1.0
CZ B:ARG78 4.4 53.0 1.0
CG A:PHE105 4.6 32.2 1.0
CG B:LEU79 4.7 46.7 1.0
O B:ARG78 4.7 37.1 1.0
CA B:LEU79 4.7 36.5 1.0
C5 A:ZLL302 4.7 107.5 1.0
NE B:ARG78 4.8 46.9 1.0
N B:LEU79 4.8 33.2 1.0
NH2 B:ARG78 4.8 53.3 1.0
O A:LEU104 4.8 25.6 1.0
C B:ARG78 4.8 34.4 1.0
C A:LEU104 4.9 30.0 1.0
CB B:GLU82 4.9 44.6 1.0
CD B:GLU82 5.0 52.3 1.0
CB A:SER108 5.0 41.8 1.0

Bromine binding site 3 out of 14 in 8hgk

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Bromine binding site 3 out of 14 in the Crystal Structure of Human Clpp in Complex with ZK53


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 in Complex with ZK53 within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Br301

b:170.9
occ:1.00
BR1 C:ZLL301 0.0 170.9 1.0
C2 C:ZLL301 1.9 128.0 1.0
C3 C:ZLL301 2.9 102.8 1.0
C7 C:ZLL301 3.0 115.3 1.0
CD2 C:LEU79 3.5 48.2 1.0
CA B:PHE105 3.8 32.6 1.0
CB B:PHE105 4.0 31.2 1.0
CD1 B:PHE105 4.1 30.9 1.0
C4 C:ZLL301 4.2 101.6 1.0
CG C:ARG78 4.2 38.8 1.0
N B:PHE105 4.2 33.2 1.0
C6 C:ZLL301 4.3 107.4 1.0
OG B:SER108 4.3 34.6 1.0
NH1 C:ARG78 4.4 48.0 1.0
CG C:LEU79 4.5 42.5 1.0
CG B:PHE105 4.6 31.3 1.0
CA C:LEU79 4.6 32.4 1.0
O C:ARG78 4.7 25.2 1.0
N C:LEU79 4.7 31.4 1.0
CZ C:ARG78 4.7 47.5 1.0
C B:LEU104 4.7 33.6 1.0
O B:LEU104 4.7 27.6 1.0
C5 C:ZLL301 4.8 105.8 1.0
CG C:GLU82 4.8 49.7 1.0
C C:ARG78 4.8 29.6 1.0
CB C:GLU82 5.0 41.9 1.0
OE1 C:GLU82 5.0 53.3 1.0

Bromine binding site 4 out of 14 in 8hgk

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Bromine binding site 4 out of 14 in the Crystal Structure of Human Clpp in Complex with ZK53


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 in Complex with ZK53 within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Br301

b:146.9
occ:1.00
BR1 D:ZLL301 0.0 146.9 1.0
C2 D:ZLL301 1.9 92.4 1.0
C3 D:ZLL301 2.8 81.0 1.0
C7 D:ZLL301 2.9 82.5 1.0
CA C:PHE105 3.9 29.7 1.0
CD1 D:LEU79 3.9 46.7 1.0
CD1 C:PHE105 3.9 30.9 1.0
OG C:SER108 4.0 28.6 1.0
CG D:ARG78 4.0 29.4 1.0
CB C:PHE105 4.1 29.1 1.0
C4 D:ZLL301 4.1 85.7 1.0
CG D:GLU82 4.2 41.8 1.0
C6 D:ZLL301 4.2 84.5 1.0
NH1 D:ARG78 4.3 43.1 1.0
CZ D:ARG78 4.4 41.8 1.0
N C:PHE105 4.4 26.9 1.0
CG C:PHE105 4.5 31.4 1.0
NE D:ARG78 4.6 35.6 1.0
NH2 D:ARG78 4.7 47.8 1.0
C5 D:ZLL301 4.7 86.3 1.0
CB C:SER108 4.8 33.8 1.0
O D:ARG78 4.8 24.2 1.0
O C:LEU104 4.8 25.4 1.0
C C:LEU104 4.9 25.4 1.0
CG D:LEU79 4.9 40.8 1.0
CD D:ARG78 4.9 33.2 1.0
C D:ARG78 4.9 23.9 1.0
CA D:LEU79 4.9 30.0 1.0
CE1 C:PHE105 4.9 31.6 1.0
N D:LEU79 5.0 28.8 1.0

Bromine binding site 5 out of 14 in 8hgk

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Bromine binding site 5 out of 14 in the Crystal Structure of Human Clpp in Complex with ZK53


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 in Complex with ZK53 within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Br301

b:157.3
occ:1.00
BR1 E:ZLL301 0.0 157.3 1.0
C2 E:ZLL301 1.9 108.3 1.0
C3 E:ZLL301 2.8 102.1 1.0
C7 E:ZLL301 3.0 105.4 1.0
O E:HOH462 3.2 37.7 1.0
CA D:PHE105 3.9 26.4 1.0
CD2 E:LEU79 4.0 41.2 1.0
OG D:SER108 4.0 42.1 1.0
CG E:GLU82 4.0 45.1 1.0
C4 E:ZLL301 4.1 104.3 1.0
C6 E:ZLL301 4.2 105.9 1.0
N D:PHE105 4.3 23.2 1.0
O D:LEU104 4.4 24.7 1.0
CB D:PHE105 4.4 27.9 1.0
CZ E:ARG78 4.5 45.4 1.0
CB D:SER108 4.5 39.2 1.0
NH1 E:ARG78 4.5 50.4 1.0
CG E:ARG78 4.5 30.9 1.0
CD1 D:PHE105 4.5 34.0 1.0
C D:LEU104 4.6 25.6 1.0
NH2 E:ARG78 4.6 48.4 1.0
C5 E:ZLL301 4.7 102.4 1.0
NE E:ARG78 4.8 40.5 1.0
CB E:GLU82 4.8 36.5 1.0

Bromine binding site 6 out of 14 in 8hgk

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Bromine binding site 6 out of 14 in the Crystal Structure of Human Clpp in Complex with ZK53


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 in Complex with ZK53 within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Br301

b:155.6
occ:1.00
BR1 F:ZLL301 0.0 155.6 1.0
C2 F:ZLL301 1.9 120.0 1.0
C3 F:ZLL301 2.9 102.6 1.0
C7 F:ZLL301 3.0 106.1 1.0
CD2 F:LEU79 3.7 45.1 1.0
CA E:PHE105 3.9 25.4 1.0
CB E:PHE105 4.1 26.8 1.0
CG F:ARG78 4.1 35.9 1.0
CD1 E:PHE105 4.1 31.1 1.0
C4 F:ZLL301 4.2 88.8 1.0
C6 F:ZLL301 4.3 100.0 1.0
N E:PHE105 4.3 23.5 1.0
OG E:SER108 4.4 35.0 1.0
NH1 F:ARG78 4.4 51.5 1.0
CG F:GLU82 4.5 42.4 1.0
CZ F:ARG78 4.6 53.2 1.0
CG E:PHE105 4.6 29.3 1.0
CA F:LEU79 4.6 29.0 1.0
CG F:LEU79 4.7 40.1 1.0
O F:ARG78 4.7 26.9 1.0
N F:LEU79 4.7 29.1 1.0
C5 F:ZLL301 4.8 96.6 1.0
C F:ARG78 4.8 29.8 1.0
C E:LEU104 4.8 24.7 1.0
O E:LEU104 4.8 23.0 1.0
NE F:ARG78 4.9 48.2 1.0
CB F:GLU82 4.9 34.4 1.0
NH2 F:ARG78 5.0 59.2 1.0

Bromine binding site 7 out of 14 in 8hgk

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Bromine binding site 7 out of 14 in the Crystal Structure of Human Clpp in Complex with ZK53


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 in Complex with ZK53 within 5.0Å range:
probe atom residue distance (Å) B Occ
G:Br301

b:167.5
occ:1.00
BR1 G:ZLL301 0.0 167.5 1.0
C2 G:ZLL301 1.9 119.1 1.0
C3 G:ZLL301 2.8 109.2 1.0
C7 G:ZLL301 2.9 104.8 1.0
CD1 G:LEU79 3.5 42.3 1.0
CA F:PHE105 3.7 28.6 1.0
CB F:PHE105 3.9 29.4 1.0
CG G:ARG78 4.0 34.5 1.0
CD1 F:PHE105 4.0 32.7 1.0
C4 G:ZLL301 4.2 103.5 1.0
N F:PHE105 4.2 25.9 1.0
C6 G:ZLL301 4.3 99.8 1.0
CG G:GLU82 4.3 47.4 1.0
OG F:SER108 4.3 37.4 1.0
CG F:PHE105 4.4 31.7 1.0
CZ G:ARG78 4.5 45.8 1.0
NH1 G:ARG78 4.5 47.1 1.0
CG G:LEU79 4.5 41.1 1.0
C F:LEU104 4.7 26.7 1.0
CA G:LEU79 4.7 32.1 1.0
O G:ARG78 4.7 30.3 1.0
NE G:ARG78 4.7 43.2 1.0
N G:LEU79 4.7 29.3 1.0
O F:LEU104 4.7 29.2 1.0
C5 G:ZLL301 4.7 95.6 1.0
C G:ARG78 4.8 29.7 1.0
CB G:ARG78 4.9 30.3 1.0
NH2 G:ARG78 4.9 52.0 1.0
CD G:ARG78 5.0 40.3 1.0
C F:PHE105 5.0 28.3 1.0

Bromine binding site 8 out of 14 in 8hgk

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Bromine binding site 8 out of 14 in the Crystal Structure of Human Clpp in Complex with ZK53


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 8 of Crystal Structure of Human Clpp in Complex with ZK53 within 5.0Å range:
probe atom residue distance (Å) B Occ
H:Br301

b:183.5
occ:1.00
BR1 H:ZLL301 0.0 183.5 1.0
C2 H:ZLL301 1.9 131.6 1.0
C3 H:ZLL301 2.9 120.4 1.0
C7 H:ZLL301 3.0 116.9 1.0
CD1 H:LEU79 3.8 48.7 1.0
CA N:PHE105 3.9 33.9 1.0
CD1 N:PHE105 3.9 35.5 1.0
CG H:ARG78 4.0 43.2 1.0
CB N:PHE105 4.1 33.2 1.0
OG N:SER108 4.1 40.2 1.0
C4 H:ZLL301 4.2 117.0 1.0
NH1 H:ARG78 4.2 59.5 1.0
C6 H:ZLL301 4.3 115.0 1.0
CZ H:ARG78 4.3 57.6 1.0
OE2 H:GLU82 4.4 55.5 1.0
N N:PHE105 4.4 34.1 1.0
CG N:PHE105 4.5 33.4 1.0
NE H:ARG78 4.6 52.3 1.0
O H:ARG78 4.7 27.1 1.0
CG H:GLU82 4.7 56.0 1.0
NH2 H:ARG78 4.7 59.9 1.0
C5 H:ZLL301 4.8 113.6 1.0
CG H:LEU79 4.8 46.7 1.0
CA H:LEU79 4.8 36.6 1.0
C H:ARG78 4.8 33.6 1.0
O N:LEU104 4.8 31.4 1.0
N H:LEU79 4.8 34.0 1.0
CB N:SER108 4.9 40.1 1.0
C N:LEU104 4.9 34.3 1.0
CB H:GLU82 4.9 48.3 1.0
CD H:ARG78 4.9 50.4 1.0
CE1 N:PHE105 5.0 34.8 1.0

Bromine binding site 9 out of 14 in 8hgk

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Bromine binding site 9 out of 14 in the Crystal Structure of Human Clpp in Complex with ZK53


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 9 of Crystal Structure of Human Clpp in Complex with ZK53 within 5.0Å range:
probe atom residue distance (Å) B Occ
I:Br301

b:171.0
occ:1.00
BR1 I:ZLL301 0.0 171.0 1.0
C2 I:ZLL301 1.9 124.3 1.0
C3 I:ZLL301 2.8 112.7 1.0
C7 I:ZLL301 3.0 109.1 1.0
CA H:PHE105 3.9 34.1 1.0
CD1 I:LEU79 3.9 46.1 1.0
CD1 H:PHE105 4.0 35.0 1.0
OG H:SER108 4.0 51.8 1.0
CG I:GLU82 4.0 53.1 1.0
CG I:ARG78 4.1 39.3 1.0
CB H:PHE105 4.1 34.6 1.0
C4 I:ZLL301 4.1 109.4 1.0
C6 I:ZLL301 4.3 85.0 1.0
N H:PHE105 4.4 33.0 1.0
NH1 I:ARG78 4.4 51.6 1.0
CG H:PHE105 4.5 34.9 1.0
CZ I:ARG78 4.6 51.1 1.0
O I:ARG78 4.7 31.1 1.0
C5 I:ZLL301 4.7 97.3 1.0
CB H:SER108 4.8 45.7 1.0
O H:LEU104 4.8 40.0 1.0
C H:LEU104 4.8 36.6 1.0
CG I:LEU79 4.8 43.8 1.0
NE I:ARG78 4.9 47.8 1.0
CA I:LEU79 4.9 35.1 1.0
C I:ARG78 4.9 33.1 1.0
CD I:GLU82 4.9 53.3 1.0
N I:LEU79 4.9 34.2 1.0

Bromine binding site 10 out of 14 in 8hgk

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Bromine binding site 10 out of 14 in the Crystal Structure of Human Clpp in Complex with ZK53


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 10 of Crystal Structure of Human Clpp in Complex with ZK53 within 5.0Å range:
probe atom residue distance (Å) B Occ
J:Br301

b:160.1
occ:1.00
BR1 J:ZLL301 0.0 160.1 1.0
C2 J:ZLL301 1.9 96.8 1.0
C3 J:ZLL301 2.9 79.9 1.0
C7 J:ZLL301 2.9 88.2 1.0
CD1 I:PHE105 3.8 33.0 1.0
CG J:ARG78 3.9 40.3 1.0
CD2 J:LEU79 3.9 42.9 1.0
CA I:PHE105 4.0 31.6 1.0
CB I:PHE105 4.1 31.1 1.0
OG I:SER108 4.2 40.2 1.0
C4 J:ZLL301 4.2 88.6 1.0
C6 J:ZLL301 4.3 90.4 1.0
CG J:GLU82 4.3 46.5 1.0
NE J:ARG78 4.5 51.1 1.0
CG I:PHE105 4.5 32.8 1.0
CZ J:ARG78 4.5 54.3 1.0
N I:PHE105 4.6 28.0 1.0
O J:ARG78 4.6 26.9 1.0
NH2 J:ARG78 4.7 59.3 1.0
C J:ARG78 4.7 28.7 1.0
CA J:LEU79 4.7 32.5 1.0
C5 J:ZLL301 4.7 84.3 1.0
N J:LEU79 4.8 30.3 1.0
CD J:ARG78 4.8 45.9 1.0
NH1 J:ARG78 4.8 61.6 1.0
CE1 I:PHE105 4.8 33.9 1.0
CG J:LEU79 4.9 41.5 1.0
CB J:ARG78 4.9 36.9 1.0
CB I:SER108 5.0 37.8 1.0

Reference:

C.-G.Yang, J.H.Gan, L.-L.Zhou. Crystal Structure of Human Clpp in Complex with ZK53 To Be Published.
Page generated: Thu Jul 11 05:14:55 2024

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