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Chlorine in PDB 6pxa: The Crystal Structure of Chloramphenicol Acetyltransferase-Like Protein From Vibrio Fischeri ES114 in Complex with Taurocholic Acid

Enzymatic activity of The Crystal Structure of Chloramphenicol Acetyltransferase-Like Protein From Vibrio Fischeri ES114 in Complex with Taurocholic Acid

All present enzymatic activity of The Crystal Structure of Chloramphenicol Acetyltransferase-Like Protein From Vibrio Fischeri ES114 in Complex with Taurocholic Acid:
2.3.1.28;

Protein crystallography data

The structure of The Crystal Structure of Chloramphenicol Acetyltransferase-Like Protein From Vibrio Fischeri ES114 in Complex with Taurocholic Acid, PDB code: 6pxa was solved by K.Tan, N.Maltseva, R.Jedrzejczak, M.Kuhn, A.Joachimiak, Center Forstructural Genomics Of Infectious Diseases (Csgid), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 46.90 / 1.82
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 43.519, 121.363, 146.170, 89.40, 89.91, 87.60
R / Rfree (%) 19.7 / 23.8

Chlorine Binding Sites:

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 16;

Binding sites:

The binding sites of Chlorine atom in the The Crystal Structure of Chloramphenicol Acetyltransferase-Like Protein From Vibrio Fischeri ES114 in Complex with Taurocholic Acid (pdb code 6pxa). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 16 binding sites of Chlorine where determined in the The Crystal Structure of Chloramphenicol Acetyltransferase-Like Protein From Vibrio Fischeri ES114 in Complex with Taurocholic Acid, PDB code: 6pxa:
Jump to Chlorine binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Chlorine binding site 1 out of 16 in 6pxa

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Chlorine binding site 1 out of 16 in the The Crystal Structure of Chloramphenicol Acetyltransferase-Like Protein From Vibrio Fischeri ES114 in Complex with Taurocholic Acid


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of The Crystal Structure of Chloramphenicol Acetyltransferase-Like Protein From Vibrio Fischeri ES114 in Complex with Taurocholic Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl302

b:56.4
occ:1.00
 OH A:TYR29 3.2 44.4 1.0
NE2 C:HIS90 3.2 49.3 1.0
OG A:SER31 3.3 36.2 0.7
CE1 A:TYR29 3.9 49.2 1.0
CE1 C:HIS90 3.9 45.2 1.0
CZ A:TYR29 4.0 46.4 1.0
CB A:SER31 4.2 39.1 0.3
CB A:SER31 4.2 39.2 0.7
CD2 C:HIS90 4.3 46.6 1.0
C18 C:TCH301 4.3 85.0 1.0
C20 C:TCH301 4.5 64.7 1.0
OE1 C:GLN88 4.5 46.9 1.0
CB A:ALA77 4.5 40.6 1.0
OG A:SER31 4.5 36.6 0.3
O C:HOH410 4.6 40.2 1.0
CA A:ALA77 4.6 39.1 1.0
C16 C:TCH301 4.9 79.1 1.0
CB A:SER75 4.9 36.1 1.0
NE1 A:TRP126 4.9 43.5 1.0
N A:ALA77 5.0 36.0 1.0

Chlorine binding site 2 out of 16 in 6pxa

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Chlorine binding site 2 out of 16 in the The Crystal Structure of Chloramphenicol Acetyltransferase-Like Protein From Vibrio Fischeri ES114 in Complex with Taurocholic Acid


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of The Crystal Structure of Chloramphenicol Acetyltransferase-Like Protein From Vibrio Fischeri ES114 in Complex with Taurocholic Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl302

b:52.1
occ:1.00
 OH B:TYR29 3.1 44.1 1.0
OG B:SER31 3.3 43.6 1.0
NE2 A:HIS90 3.3 49.1 1.0
CZ3 B:TRP126 3.6 39.5 0.2
CE2 B:TYR29 3.9 41.3 1.0
CZ B:TYR29 3.9 39.8 1.0
CH2 B:TRP126 4.0 41.0 0.2
CE1 A:HIS90 4.0 40.5 1.0
C18 A:TCH301 4.1 66.5 1.0
OE1 A:GLN88 4.2 62.0 1.0
CB B:SER31 4.3 43.9 1.0
CD2 A:HIS90 4.4 45.2 1.0
C20 A:TCH301 4.4 55.9 1.0
CB B:ALA77 4.5 33.4 1.0
C16 A:TCH301 4.6 59.2 1.0
CA B:ALA77 4.6 33.8 1.0
O A:HOH402 4.6 41.0 1.0
CE3 B:TRP126 4.7 38.4 0.2
NE1 B:TRP126 4.9 37.7 0.8
N B:ALA77 5.0 35.9 1.0
CB B:SER75 5.0 42.7 1.0
C17 A:TCH301 5.0 60.8 1.0

Chlorine binding site 3 out of 16 in 6pxa

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Chlorine binding site 3 out of 16 in the The Crystal Structure of Chloramphenicol Acetyltransferase-Like Protein From Vibrio Fischeri ES114 in Complex with Taurocholic Acid


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of The Crystal Structure of Chloramphenicol Acetyltransferase-Like Protein From Vibrio Fischeri ES114 in Complex with Taurocholic Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cl302

b:45.8
occ:1.00
 O B:HOH407 3.0 44.1 1.0
OH C:TYR29 3.1 41.3 1.0
NE2 B:HIS90 3.2 38.7 1.0
OG C:SER31 3.2 31.6 0.6
CE1 C:TYR29 3.8 45.0 1.0
CE1 B:HIS90 3.9 38.2 1.0
CZ C:TYR29 3.9 39.9 1.0
CB C:SER31 4.1 32.9 0.6
OE1 B:GLN88 4.1 58.9 1.0
CB C:SER31 4.1 33.2 0.4
C18 B:TCH301 4.1 58.5 1.0
CD2 B:HIS90 4.3 38.9 1.0
OG C:SER31 4.5 38.0 0.4
C20 B:TCH301 4.5 51.8 1.0
CB C:ALA77 4.6 36.8 1.0
CA C:ALA77 4.6 40.5 1.0
O B:HOH405 4.6 34.4 1.0
C16 B:TCH301 4.8 54.2 1.0
CB C:SER75 4.9 35.6 1.0
N C:ALA77 4.9 32.3 1.0

Chlorine binding site 4 out of 16 in 6pxa

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Chlorine binding site 4 out of 16 in the The Crystal Structure of Chloramphenicol Acetyltransferase-Like Protein From Vibrio Fischeri ES114 in Complex with Taurocholic Acid


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of The Crystal Structure of Chloramphenicol Acetyltransferase-Like Protein From Vibrio Fischeri ES114 in Complex with Taurocholic Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Cl302

b:54.0
occ:1.00
 OH D:TYR29 3.0 45.2 1.0
NE2 F:HIS90 3.2 45.0 1.0
O F:HOH423 3.2 43.5 1.0
OG D:SER31 3.3 40.4 1.0
CE1 D:TYR29 3.8 51.1 1.0
CE1 F:HIS90 3.9 44.3 1.0
CZ D:TYR29 3.9 46.3 1.0
CD2 F:HIS90 4.3 43.7 1.0
CB D:SER31 4.3 42.5 1.0
C18 F:TCH301 4.3 73.5 1.0
OE1 F:GLN88 4.5 49.8 1.0
C20 F:TCH301 4.5 69.0 1.0
CB D:ALA77 4.5 32.7 1.0
O F:HOH412 4.6 35.1 1.0
C16 F:TCH301 4.7 68.5 1.0
CA D:ALA77 4.7 41.1 1.0
CB D:SER75 4.9 37.1 1.0
NE1 D:TRP126 5.0 38.8 1.0
C22 F:TCH301 5.0 71.5 1.0

Chlorine binding site 5 out of 16 in 6pxa

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Chlorine binding site 5 out of 16 in the The Crystal Structure of Chloramphenicol Acetyltransferase-Like Protein From Vibrio Fischeri ES114 in Complex with Taurocholic Acid


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 5 of The Crystal Structure of Chloramphenicol Acetyltransferase-Like Protein From Vibrio Fischeri ES114 in Complex with Taurocholic Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Cl302

b:62.0
occ:1.00
 OH E:TYR29 3.0 46.5 1.0
O D:HOH411 3.0 48.0 1.0
NE2 D:HIS90 3.2 50.9 1.0
OG E:SER31 3.3 42.1 1.0
O E:HOH430 3.4 57.2 1.0
CE2 E:TYR29 3.8 49.2 1.0
CZ E:TYR29 3.9 51.7 1.0
CE1 D:HIS90 4.0 51.2 1.0
CB E:SER31 4.1 37.9 1.0
C18 D:TCH301 4.2 58.4 1.0
CD2 D:HIS90 4.3 50.4 1.0
OE1 D:GLN88 4.4 57.0 1.0
C20 D:TCH301 4.4 59.6 1.0
O D:HOH424 4.5 37.8 1.0
CB E:ALA77 4.6 44.7 1.0
CA E:ALA77 4.7 41.4 1.0
C16 D:TCH301 4.7 53.6 1.0
CB E:SER75 5.0 43.2 1.0
NE1 E:TRP126 5.0 43.2 1.0

Chlorine binding site 6 out of 16 in 6pxa

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Chlorine binding site 6 out of 16 in the The Crystal Structure of Chloramphenicol Acetyltransferase-Like Protein From Vibrio Fischeri ES114 in Complex with Taurocholic Acid


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 6 of The Crystal Structure of Chloramphenicol Acetyltransferase-Like Protein From Vibrio Fischeri ES114 in Complex with Taurocholic Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Cl302

b:45.5
occ:1.00
 O E:HOH402 2.9 41.7 1.0
OH F:TYR29 3.1 36.3 1.0
OG F:SER31 3.1 33.6 0.6
O F:HOH450 3.2 45.1 1.0
NE2 E:HIS90 3.2 40.9 1.0
CE1 F:TYR29 3.8 47.3 1.0
CZ F:TYR29 3.9 43.5 1.0
CB F:SER31 3.9 39.1 0.4
CE1 E:HIS90 4.0 40.3 1.0
CB F:SER31 4.0 39.4 0.6
OE1 E:GLN88 4.1 55.7 1.0
C18 E:TCH301 4.1 61.0 1.0
OG F:SER31 4.3 46.6 0.4
CD2 E:HIS90 4.3 39.7 1.0
C20 E:TCH301 4.4 42.0 1.0
O E:HOH408 4.5 34.1 1.0
CB F:ALA77 4.5 39.9 1.0
CA F:ALA77 4.6 35.3 1.0
C16 E:TCH301 4.8 61.2 1.0

Chlorine binding site 7 out of 16 in 6pxa

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Chlorine binding site 7 out of 16 in the The Crystal Structure of Chloramphenicol Acetyltransferase-Like Protein From Vibrio Fischeri ES114 in Complex with Taurocholic Acid


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 7 of The Crystal Structure of Chloramphenicol Acetyltransferase-Like Protein From Vibrio Fischeri ES114 in Complex with Taurocholic Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Cl303

b:0.5
occ:1.00
 OE1 F:GLU130 3.5 43.4 1.0
OE2 E:GLU130 3.7 41.0 1.0
NE F:ARG148 3.9 39.2 1.0
NH2 F:ARG148 4.0 43.9 1.0
NE E:ARG148 4.0 40.3 1.0
OE2 D:GLU130 4.0 44.8 1.0
CZ F:ARG148 4.1 41.9 1.0
NE D:ARG148 4.1 41.4 1.0
NH2 D:ARG148 4.3 39.9 1.0
NH2 E:ARG148 4.3 44.4 1.0
CZ E:ARG148 4.3 45.5 1.0
CZ D:ARG148 4.3 43.8 1.0
CD F:GLU130 4.5 45.0 1.0
CD E:GLU130 4.6 44.5 1.0
CD E:ARG148 4.7 35.2 1.0
CD F:ARG148 4.8 33.3 1.0
CD D:GLU130 4.8 48.7 1.0
CD D:ARG148 4.9 36.9 1.0
NH1 F:ARG148 5.0 43.6 1.0

Chlorine binding site 8 out of 16 in 6pxa

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Chlorine binding site 8 out of 16 in the The Crystal Structure of Chloramphenicol Acetyltransferase-Like Protein From Vibrio Fischeri ES114 in Complex with Taurocholic Acid


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 8 of The Crystal Structure of Chloramphenicol Acetyltransferase-Like Protein From Vibrio Fischeri ES114 in Complex with Taurocholic Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
G:Cl302

b:44.8
occ:1.00
 OH G:TYR29 3.1 41.6 1.0
O I:HOH412 3.2 41.7 1.0
NE2 I:HIS90 3.2 39.3 1.0
OG G:SER31 3.3 40.5 1.0
CE1 G:TYR29 3.9 44.0 1.0
CE1 I:HIS90 3.9 39.4 1.0
CZ G:TYR29 4.0 44.0 1.0
C18 I:TCH301 4.0 60.2 1.0
OE1 I:GLN88 4.2 57.5 1.0
CB G:SER31 4.2 34.4 1.0
CD2 I:HIS90 4.3 35.9 1.0
C20 I:TCH301 4.5 62.4 1.0
O I:HOH428 4.5 32.5 1.0
CB G:ALA77 4.6 35.6 1.0
CA G:ALA77 4.8 37.2 1.0
C16 I:TCH301 4.8 57.1 1.0
CB G:SER75 4.9 37.0 1.0

Chlorine binding site 9 out of 16 in 6pxa

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Chlorine binding site 9 out of 16 in the The Crystal Structure of Chloramphenicol Acetyltransferase-Like Protein From Vibrio Fischeri ES114 in Complex with Taurocholic Acid


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 9 of The Crystal Structure of Chloramphenicol Acetyltransferase-Like Protein From Vibrio Fischeri ES114 in Complex with Taurocholic Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
G:Cl303

b:53.0
occ:1.00
 OH H:TYR29 3.1 40.8 1.0
NE2 G:HIS90 3.3 43.0 1.0
CE1 H:TYR29 3.7 40.7 1.0
CB H:SER31 3.8 37.0 1.0
CZ H:TYR29 3.9 41.2 1.0
CE1 G:HIS90 4.0 45.4 1.0
OG H:SER31 4.1 60.4 1.0
CB H:ALA77 4.2 38.2 1.0
C18 G:TCH301 4.3 70.5 1.0
O G:HOH433 4.3 35.2 1.0
CA H:ALA77 4.4 35.3 1.0
C20 G:TCH301 4.4 60.6 1.0
OE1 G:GLN88 4.4 47.5 1.0
CD2 G:HIS90 4.5 44.1 1.0
C16 G:TCH301 4.6 58.9 1.0
N H:ALA77 4.7 36.0 1.0
O H:ILE76 4.9 36.3 1.0
C22 G:TCH301 4.9 67.3 1.0
C H:ILE76 4.9 34.8 1.0
NE1 H:TRP126 5.0 41.7 1.0

Chlorine binding site 10 out of 16 in 6pxa

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Chlorine binding site 10 out of 16 in the The Crystal Structure of Chloramphenicol Acetyltransferase-Like Protein From Vibrio Fischeri ES114 in Complex with Taurocholic Acid


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 10 of The Crystal Structure of Chloramphenicol Acetyltransferase-Like Protein From Vibrio Fischeri ES114 in Complex with Taurocholic Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
G:Cl304

b:76.3
occ:1.00
 O G:TRP188 3.4 39.6 1.0
CD1 G:ILE193 3.8 47.7 1.0
O G:TRP186 4.1 47.1 1.0
N G:LEU190 4.2 48.4 1.0
CA G:LEU190 4.3 45.4 1.0
NZ G:LYS72 4.4 60.5 1.0
CB G:LEU190 4.4 43.4 1.0
C G:TRP188 4.6 40.2 1.0
CE2 G:TYR27 4.6 47.4 1.0
C G:PRO189 4.7 43.2 1.0
OD2 G:ASP26 4.7 69.0 1.0
CD1 G:LEU190 4.8 48.4 1.0
CZ G:PHE73 4.8 47.5 1.0
CE2 G:PHE73 4.9 48.5 1.0
CG1 G:ILE193 5.0 41.4 1.0

Reference:

K.Tan, N.Maltseva, R.Jedrzejczak, M.Kuhn, A.Joachimiak. The Crystal Structure of Chloramphenicol Acetyltransferase-Like Protein From Vibrio Fischeri ES114 in Complex with Taurocholic Acid To Be Published.
Page generated: Mon Jul 29 13:38:55 2024

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