Chlorine in PDB 1qhs: Chloramphenicol Phosphotransferase in Complex with Chloramphenicol From Streptomyces Venezuelae
Protein crystallography data
The structure of Chloramphenicol Phosphotransferase in Complex with Chloramphenicol From Streptomyces Venezuelae, PDB code: 1qhs
was solved by
T.Izard,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
99.00 /
2.80
|
Space group
|
I 41 3 2
|
Cell size a, b, c (Å), α, β, γ (°)
|
200.000,
200.000,
200.000,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
22.6 /
23.8
|
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Chloramphenicol Phosphotransferase in Complex with Chloramphenicol From Streptomyces Venezuelae
(pdb code 1qhs). This binding sites where shown within
5.0 Angstroms radius around Chlorine atom.
In total 4 binding sites of Chlorine where determined in the
Chloramphenicol Phosphotransferase in Complex with Chloramphenicol From Streptomyces Venezuelae, PDB code: 1qhs:
Jump to Chlorine binding site number:
1;
2;
3;
4;
Chlorine binding site 1 out
of 4 in 1qhs
Go back to
Chlorine Binding Sites List in 1qhs
Chlorine binding site 1 out
of 4 in the Chloramphenicol Phosphotransferase in Complex with Chloramphenicol From Streptomyces Venezuelae
 Mono view
 Stereo pair view
|
A full contact list of Chlorine with other atoms in the Cl binding
site number 1 of Chloramphenicol Phosphotransferase in Complex with Chloramphenicol From Streptomyces Venezuelae within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cl999
b:31.6
occ:1.00
|
CL1
|
A:CLM999
|
0.0
|
31.6
|
1.0
|
C1
|
A:CLM999
|
1.7
|
31.6
|
1.0
|
C2
|
A:CLM999
|
2.7
|
31.6
|
1.0
|
CL2
|
A:CLM999
|
2.8
|
31.6
|
1.0
|
O2
|
A:CLM999
|
3.2
|
31.6
|
1.0
|
CZ
|
A:PHE56
|
3.4
|
41.9
|
1.0
|
N2
|
A:CLM999
|
3.6
|
31.6
|
1.0
|
O
|
A:HOH1029
|
3.8
|
27.2
|
1.0
|
O
|
A:HOH1010
|
3.9
|
38.0
|
1.0
|
CD1
|
A:ILE40
|
3.9
|
23.6
|
1.0
|
O
|
A:HOH1015
|
4.0
|
23.6
|
1.0
|
CE2
|
A:PHE56
|
4.0
|
41.9
|
1.0
|
CE1
|
A:PHE56
|
4.0
|
41.9
|
1.0
|
CG2
|
A:ILE40
|
4.2
|
23.6
|
1.0
|
O
|
A:HOH1006
|
4.4
|
29.8
|
1.0
|
OD1
|
A:ASP37
|
4.7
|
33.2
|
1.0
|
C7
|
A:CLM999
|
4.8
|
31.6
|
1.0
|
CB
|
A:ILE40
|
4.9
|
23.6
|
1.0
|
C3
|
A:CLM999
|
4.9
|
31.6
|
1.0
|
CG1
|
A:ILE40
|
5.0
|
23.6
|
1.0
|
|
Chlorine binding site 2 out
of 4 in 1qhs
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Chlorine Binding Sites List in 1qhs
Chlorine binding site 2 out
of 4 in the Chloramphenicol Phosphotransferase in Complex with Chloramphenicol From Streptomyces Venezuelae
 Mono view
 Stereo pair view
|
A full contact list of Chlorine with other atoms in the Cl binding
site number 2 of Chloramphenicol Phosphotransferase in Complex with Chloramphenicol From Streptomyces Venezuelae within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cl999
b:31.6
occ:1.00
|
CL2
|
A:CLM999
|
0.0
|
31.6
|
1.0
|
C1
|
A:CLM999
|
1.8
|
31.6
|
1.0
|
C2
|
A:CLM999
|
2.7
|
31.6
|
1.0
|
CL1
|
A:CLM999
|
2.8
|
31.6
|
1.0
|
O2
|
A:CLM999
|
2.9
|
31.6
|
1.0
|
O
|
A:HOH1015
|
3.5
|
23.6
|
1.0
|
NH2
|
A:ARG136
|
3.6
|
35.3
|
1.0
|
CZ
|
A:ARG136
|
3.7
|
35.3
|
1.0
|
N2
|
A:CLM999
|
3.8
|
31.6
|
1.0
|
O
|
A:HOH1029
|
3.8
|
27.2
|
1.0
|
O
|
A:HOH1044
|
4.0
|
28.7
|
1.0
|
NH1
|
A:ARG136
|
4.0
|
35.3
|
1.0
|
O
|
A:HOH1006
|
4.0
|
29.8
|
1.0
|
NE
|
A:ARG136
|
4.1
|
35.3
|
1.0
|
OD1
|
A:ASP37
|
4.4
|
33.2
|
1.0
|
CG
|
A:ASP37
|
4.6
|
33.2
|
1.0
|
OD2
|
A:ASP37
|
4.8
|
33.2
|
1.0
|
O
|
A:HOH1010
|
4.8
|
38.0
|
1.0
|
CD
|
A:ARG136
|
4.9
|
35.3
|
1.0
|
|
Chlorine binding site 3 out
of 4 in 1qhs
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Chlorine Binding Sites List in 1qhs
Chlorine binding site 3 out
of 4 in the Chloramphenicol Phosphotransferase in Complex with Chloramphenicol From Streptomyces Venezuelae
 Mono view
 Stereo pair view
|
A full contact list of Chlorine with other atoms in the Cl binding
site number 3 of Chloramphenicol Phosphotransferase in Complex with Chloramphenicol From Streptomyces Venezuelae within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cl888
b:28.8
occ:0.50
|
CL1
|
A:CLM888
|
0.0
|
28.8
|
0.5
|
C1
|
A:CLM888
|
1.7
|
28.8
|
0.5
|
C2
|
A:CLM888
|
2.7
|
28.8
|
0.5
|
CL2
|
A:CLM888
|
2.8
|
28.8
|
0.5
|
O2
|
A:CLM888
|
3.2
|
28.8
|
0.5
|
CB
|
A:LYS46
|
3.4
|
34.6
|
1.0
|
N2
|
A:CLM888
|
3.5
|
28.8
|
0.5
|
O
|
A:LYS46
|
3.5
|
40.4
|
1.0
|
CB
|
A:ALA50
|
3.6
|
33.8
|
1.0
|
CD
|
A:LYS46
|
3.8
|
34.6
|
1.0
|
CG
|
A:LYS46
|
4.0
|
34.6
|
1.0
|
C
|
A:LYS46
|
4.1
|
40.4
|
1.0
|
C7
|
A:CLM888
|
4.1
|
28.8
|
0.5
|
C8
|
A:CLM888
|
4.1
|
28.8
|
0.5
|
CA
|
A:LYS46
|
4.3
|
40.4
|
1.0
|
CA
|
A:ALA50
|
4.3
|
54.2
|
1.0
|
N
|
A:ALA50
|
4.4
|
54.2
|
1.0
|
O1
|
A:SO4602
|
4.5
|
44.3
|
0.5
|
O4
|
A:SO4602
|
4.6
|
44.3
|
0.5
|
C9
|
A:CLM888
|
4.6
|
28.8
|
0.5
|
C6
|
A:CLM888
|
4.6
|
28.8
|
0.5
|
C
|
A:SER49
|
4.7
|
55.7
|
1.0
|
C3
|
A:CLM888
|
4.9
|
28.8
|
0.5
|
O
|
A:SER49
|
4.9
|
55.7
|
1.0
|
N
|
A:MET47
|
5.0
|
40.2
|
1.0
|
|
Chlorine binding site 4 out
of 4 in 1qhs
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Chlorine Binding Sites List in 1qhs
Chlorine binding site 4 out
of 4 in the Chloramphenicol Phosphotransferase in Complex with Chloramphenicol From Streptomyces Venezuelae
 Mono view
 Stereo pair view
|
A full contact list of Chlorine with other atoms in the Cl binding
site number 4 of Chloramphenicol Phosphotransferase in Complex with Chloramphenicol From Streptomyces Venezuelae within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cl888
b:28.8
occ:0.50
|
CL2
|
A:CLM888
|
0.0
|
28.8
|
0.5
|
C1
|
A:CLM888
|
1.8
|
28.8
|
0.5
|
C2
|
A:CLM888
|
2.7
|
28.8
|
0.5
|
CL1
|
A:CLM888
|
2.8
|
28.8
|
0.5
|
O2
|
A:CLM888
|
3.1
|
28.8
|
0.5
|
N2
|
A:CLM888
|
3.7
|
28.8
|
0.5
|
O1
|
A:SO4602
|
4.4
|
44.3
|
0.5
|
|
Reference:
T.Izard,
J.Ellis.
The Crystal Structures of Chloramphenicol Phosphotransferase Reveal A Novel Inactivation Mechanism Embo J. V. 19 2690 2000.
ISSN: ISSN 0261-4189
PubMed: 10835366
DOI: 10.1093/EMBOJ/19.1.1
Page generated: Sat Jul 20 01:34:01 2024
|