Chlorine in PDB 5ux9: The Crystal Structure of Chloramphenicol Acetyltransferase From Vibrio Fischeri ES114

Enzymatic activity of The Crystal Structure of Chloramphenicol Acetyltransferase From Vibrio Fischeri ES114

All present enzymatic activity of The Crystal Structure of Chloramphenicol Acetyltransferase From Vibrio Fischeri ES114:
2.3.1.28;

Protein crystallography data

The structure of The Crystal Structure of Chloramphenicol Acetyltransferase From Vibrio Fischeri ES114, PDB code: 5ux9 was solved by K.Tan, M.Zhou, W.F.Anderson, A.Joachimiak, Center For Structural Genomicsof Infectious Diseases (Csgid), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 47.05 / 2.70
Space group P 63
Cell size a, b, c (Å), α, β, γ (°) 147.426, 147.426, 101.211, 90.00, 90.00, 120.00
R / Rfree (%) 20 / 24

Other elements in 5ux9:

The structure of The Crystal Structure of Chloramphenicol Acetyltransferase From Vibrio Fischeri ES114 also contains other interesting chemical elements:

Magnesium (Mg) 4 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the The Crystal Structure of Chloramphenicol Acetyltransferase From Vibrio Fischeri ES114 (pdb code 5ux9). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 6 binding sites of Chlorine where determined in the The Crystal Structure of Chloramphenicol Acetyltransferase From Vibrio Fischeri ES114, PDB code: 5ux9:
Jump to Chlorine binding site number: 1; 2; 3; 4; 5; 6;

Chlorine binding site 1 out of 6 in 5ux9

Go back to Chlorine Binding Sites List in 5ux9
Chlorine binding site 1 out of 6 in the The Crystal Structure of Chloramphenicol Acetyltransferase From Vibrio Fischeri ES114


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 From Vibrio Fischeri ES114 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl305

b:86.5
occ:1.00
 NE2 A:HIS90 2.8 41.9 1.0
OH B:TYR29 3.2 47.1 1.0
O B:HOH410 3.4 39.4 1.0
CE1 A:HIS90 3.6 41.4 1.0
CD2 A:HIS90 3.8 40.3 1.0
CE1 B:TYR29 4.0 46.4 1.0
OE1 A:GLN88 4.0 48.4 1.0
CZ B:TYR29 4.0 46.9 1.0
CB B:SER31 4.6 54.4 1.0
NE1 B:TRP126 4.6 34.9 1.0
CB B:ALA77 4.7 30.7 1.0
ND1 A:HIS90 4.8 41.1 1.0
O A:HOH413 4.8 32.7 1.0
CB B:SER75 4.8 38.6 1.0
CA B:ALA77 4.8 32.7 1.0
OG B:SER31 4.9 55.5 1.0
CG A:HIS90 4.9 39.9 1.0
CD A:GLN88 4.9 47.9 1.0
CB A:GLN88 4.9 46.9 1.0

Chlorine binding site 2 out of 6 in 5ux9

Go back to Chlorine Binding Sites List in 5ux9
Chlorine binding site 2 out of 6 in the The Crystal Structure of Chloramphenicol Acetyltransferase From Vibrio Fischeri ES114


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 From Vibrio Fischeri ES114 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl304

b:70.3
occ:1.00
 O B:TRP186 3.6 43.3 1.0
O B:TRP188 3.7 44.6 1.0
NZ B:LYS72 4.0 52.7 1.0
CD B:LYS72 4.5 50.0 1.0
C B:TRP186 4.8 42.8 1.0
C B:TRP188 4.8 48.5 1.0
CE B:LYS72 4.9 51.1 1.0
C B:ASP187 4.9 45.9 1.0
CE2 B:PHE73 5.0 40.4 1.0
O B:ASP187 5.0 47.7 1.0
CD1 B:ILE193 5.0 48.6 1.0
OD1 B:ASP26 5.0 75.9 1.0

Chlorine binding site 3 out of 6 in 5ux9

Go back to Chlorine Binding Sites List in 5ux9
Chlorine binding site 3 out of 6 in the The Crystal Structure of Chloramphenicol Acetyltransferase From Vibrio Fischeri ES114


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 From Vibrio Fischeri ES114 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl305

b:63.5
occ:1.00
 OD1 B:ASP111 3.3 67.7 1.0
CG B:ASP111 4.5 67.8 1.0
CA B:GLY89 4.5 47.3 1.0
CB B:PHE113 4.8 54.5 1.0
CB B:PRO99 4.9 50.2 1.0
O B:GLN88 5.0 51.8 1.0

Chlorine binding site 4 out of 6 in 5ux9

Go back to Chlorine Binding Sites List in 5ux9
Chlorine binding site 4 out of 6 in the The Crystal Structure of Chloramphenicol Acetyltransferase From Vibrio Fischeri ES114


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 From Vibrio Fischeri ES114 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl306

b:92.1
occ:1.00
 NE2 B:HIS90 2.5 46.3 1.0
O C:HOH415 3.2 36.5 1.0
CE1 B:HIS90 3.4 46.6 1.0
CD2 B:HIS90 3.5 46.2 1.0
OH C:TYR29 3.7 42.3 1.0
OE1 B:GLN88 3.9 53.1 1.0
NE1 C:TRP126 4.3 35.6 1.0
ND1 B:HIS90 4.5 45.4 1.0
CB B:GLN88 4.6 47.8 1.0
CB C:ALA77 4.6 34.7 1.0
CD B:GLN88 4.6 50.3 1.0
CG B:HIS90 4.6 46.1 1.0
CZ C:TYR29 4.7 42.7 1.0
CE1 C:TYR29 4.7 42.8 1.0
CA C:ALA77 4.9 37.9 1.0
O B:GLN88 4.9 51.8 1.0

Chlorine binding site 5 out of 6 in 5ux9

Go back to Chlorine Binding Sites List in 5ux9
Chlorine binding site 5 out of 6 in the The Crystal Structure of Chloramphenicol Acetyltransferase From Vibrio Fischeri ES114


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 From Vibrio Fischeri ES114 within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cl306

b:94.8
occ:1.00
 NE2 C:HIS90 2.7 34.1 1.0
OH A:TYR29 3.0 37.2 1.0
CE1 C:HIS90 3.4 34.9 1.0
CD2 C:HIS90 3.8 33.5 1.0
CZ A:TYR29 4.0 37.3 1.0
CE1 A:TYR29 4.1 37.2 1.0
NE1 A:TRP126 4.4 33.0 1.0
OE1 C:GLN88 4.4 36.6 1.0
CB A:ALA77 4.5 29.1 1.0
ND1 C:HIS90 4.6 34.5 1.0
CB A:SER75 4.6 36.6 1.0
CA A:ALA77 4.7 29.4 1.0
CB A:SER31 4.8 37.3 1.0
CG C:HIS90 4.8 33.7 1.0
CD1 A:TRP126 4.9 31.7 1.0
OG A:SER31 4.9 42.0 1.0
N A:ALA77 4.9 29.3 1.0

Chlorine binding site 6 out of 6 in 5ux9

Go back to Chlorine Binding Sites List in 5ux9
Chlorine binding site 6 out of 6 in the The Crystal Structure of Chloramphenicol Acetyltransferase From Vibrio Fischeri ES114


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 From Vibrio Fischeri ES114 within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Cl305

b:77.1
occ:1.00
 NE2 D:HIS90 2.7 30.6 1.0
CE1 D:HIS90 3.4 31.8 1.0
CD2 D:HIS90 3.9 29.4 1.0
NE2 D:GLN88 3.9 37.7 1.0
ND1 D:HIS90 4.7 29.8 1.0
CB D:GLN88 4.7 32.5 1.0
O D:GLN88 4.8 34.0 1.0
CD D:GLN88 4.8 37.0 1.0
CG D:HIS90 4.9 29.2 1.0

Reference:

K.Tan, M.Zhou, W.F.Anderson, A.Joachimiak. The Crystal Structure of Chloramphenicol Acetyltransferase From Vibrio Fischeri ES114 To Be Published.
Page generated: Sat Dec 12 12:32:38 2020

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