Fluorine in PDB 1kmi: Crystal Structure of An E.Coli Chemotaxis Protein, Chez
Protein crystallography data
The structure of Crystal Structure of An E.Coli Chemotaxis Protein, Chez, PDB code: 1kmi
was solved by
R.Zhao,
E.J.Collins,
R.B.Bourret,
R.E.Silversmith,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
20.00 /
2.90
|
Space group
|
P 43 21 2
|
Cell size a, b, c (Å), α, β, γ (°)
|
163.280,
163.280,
54.133,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
27.9 /
29.8
|
Other elements in 1kmi:
The structure of Crystal Structure of An E.Coli Chemotaxis Protein, Chez also contains other interesting chemical elements:
Fluorine Binding Sites:
The binding sites of Fluorine atom in the Crystal Structure of An E.Coli Chemotaxis Protein, Chez
(pdb code 1kmi). This binding sites where shown within
5.0 Angstroms radius around Fluorine atom.
In total 3 binding sites of Fluorine where determined in the
Crystal Structure of An E.Coli Chemotaxis Protein, Chez, PDB code: 1kmi:
Jump to Fluorine binding site number:
1;
2;
3;
Fluorine binding site 1 out
of 3 in 1kmi
Go back to
Fluorine Binding Sites List in 1kmi
Fluorine binding site 1 out
of 3 in the Crystal Structure of An E.Coli Chemotaxis Protein, Chez
Mono view
Stereo pair view
|
A full contact list of Fluorine with other atoms in the F binding
site number 1 of Crystal Structure of An E.Coli Chemotaxis Protein, Chez within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
Y:F201
b:0.1
occ:1.00
|
F1
|
Y:BEF201
|
0.0
|
0.1
|
1.0
|
BE
|
Y:BEF201
|
1.5
|
0.4
|
1.0
|
MG
|
Y:MG301
|
2.1
|
84.2
|
1.0
|
OD2
|
Y:ASP57
|
2.3
|
0.8
|
1.0
|
F2
|
Y:BEF201
|
2.4
|
0.2
|
1.0
|
OE1
|
Z:GLN147
|
2.4
|
88.2
|
1.0
|
F3
|
Y:BEF201
|
2.4
|
0.0
|
1.0
|
OD1
|
Y:ASP57
|
2.5
|
0.2
|
1.0
|
CG
|
Y:ASP57
|
2.7
|
0.1
|
1.0
|
CD
|
Z:GLN147
|
3.3
|
90.7
|
1.0
|
O
|
Y:ASN59
|
3.4
|
0.7
|
1.0
|
CB
|
Y:ASN59
|
3.5
|
0.3
|
1.0
|
N
|
Y:ASN59
|
3.6
|
0.8
|
1.0
|
NE2
|
Z:GLN147
|
3.6
|
88.1
|
1.0
|
CA
|
Y:ASN59
|
3.9
|
0.5
|
1.0
|
C
|
Y:ASN59
|
4.1
|
1.0
|
1.0
|
CB
|
Y:ASP57
|
4.2
|
0.1
|
1.0
|
ND2
|
Y:ASN59
|
4.3
|
0.1
|
1.0
|
OD1
|
Y:ASP13
|
4.4
|
0.2
|
1.0
|
N
|
Y:TRP58
|
4.4
|
0.0
|
1.0
|
CG
|
Y:ASN59
|
4.4
|
0.6
|
1.0
|
CG
|
Z:GLN147
|
4.6
|
93.1
|
1.0
|
C
|
Y:TRP58
|
4.6
|
0.9
|
1.0
|
NZ
|
Y:LYS109
|
4.7
|
75.4
|
1.0
|
OG1
|
Y:THR87
|
4.7
|
0.7
|
1.0
|
N
|
Y:ALA88
|
4.8
|
0.1
|
1.0
|
CA
|
Y:TRP58
|
5.0
|
0.5
|
1.0
|
CB
|
Y:ALA88
|
5.0
|
0.6
|
1.0
|
OD2
|
Y:ASP12
|
5.0
|
0.9
|
1.0
|
CB
|
Y:THR87
|
5.0
|
0.7
|
1.0
|
|
Fluorine binding site 2 out
of 3 in 1kmi
Go back to
Fluorine Binding Sites List in 1kmi
Fluorine binding site 2 out
of 3 in the Crystal Structure of An E.Coli Chemotaxis Protein, Chez
Mono view
Stereo pair view
|
A full contact list of Fluorine with other atoms in the F binding
site number 2 of Crystal Structure of An E.Coli Chemotaxis Protein, Chez within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
Y:F201
b:0.2
occ:1.00
|
F2
|
Y:BEF201
|
0.0
|
0.2
|
1.0
|
BE
|
Y:BEF201
|
1.5
|
0.4
|
1.0
|
F1
|
Y:BEF201
|
2.4
|
0.1
|
1.0
|
F3
|
Y:BEF201
|
2.4
|
0.0
|
1.0
|
OD1
|
Y:ASP57
|
2.5
|
0.2
|
1.0
|
OG1
|
Y:THR87
|
2.6
|
0.7
|
1.0
|
N
|
Y:ASN59
|
3.0
|
0.8
|
1.0
|
CB
|
Y:THR87
|
3.2
|
0.7
|
1.0
|
CG
|
Y:ASP57
|
3.3
|
0.1
|
1.0
|
N
|
Y:TRP58
|
3.3
|
0.0
|
1.0
|
CB
|
Y:TRP58
|
3.3
|
0.7
|
1.0
|
OD2
|
Y:ASP57
|
3.5
|
0.8
|
1.0
|
N
|
Y:ALA88
|
3.5
|
0.1
|
1.0
|
CA
|
Y:TRP58
|
3.6
|
0.5
|
1.0
|
CB
|
Y:ASN59
|
3.7
|
0.3
|
1.0
|
C
|
Y:TRP58
|
3.8
|
0.9
|
1.0
|
CA
|
Y:ASN59
|
4.0
|
0.5
|
1.0
|
CA
|
Y:THR87
|
4.0
|
0.5
|
1.0
|
CG
|
Y:GLU89
|
4.2
|
0.5
|
1.0
|
C
|
Y:THR87
|
4.3
|
0.1
|
1.0
|
N
|
Y:GLU89
|
4.3
|
0.9
|
1.0
|
MG
|
Y:MG301
|
4.4
|
84.2
|
1.0
|
CA
|
Y:ALA88
|
4.5
|
0.1
|
1.0
|
C
|
Y:ASP57
|
4.5
|
0.5
|
1.0
|
CB
|
Y:ALA88
|
4.5
|
0.6
|
1.0
|
CG2
|
Y:THR87
|
4.5
|
0.7
|
1.0
|
CG
|
Y:TRP58
|
4.5
|
0.8
|
1.0
|
OE1
|
Z:GLN147
|
4.5
|
88.2
|
1.0
|
CB
|
Y:ASP57
|
4.6
|
0.1
|
1.0
|
NE2
|
Z:GLN147
|
4.8
|
88.1
|
1.0
|
O
|
Y:ASN59
|
4.8
|
0.7
|
1.0
|
CA
|
Y:ASP57
|
4.9
|
0.2
|
1.0
|
C
|
Y:ALA88
|
4.9
|
0.1
|
1.0
|
C
|
Y:ASN59
|
4.9
|
1.0
|
1.0
|
OE2
|
Y:GLU89
|
4.9
|
0.4
|
1.0
|
O
|
Y:TRP58
|
5.0
|
0.7
|
1.0
|
|
Fluorine binding site 3 out
of 3 in 1kmi
Go back to
Fluorine Binding Sites List in 1kmi
Fluorine binding site 3 out
of 3 in the Crystal Structure of An E.Coli Chemotaxis Protein, Chez
Mono view
Stereo pair view
|
A full contact list of Fluorine with other atoms in the F binding
site number 3 of Crystal Structure of An E.Coli Chemotaxis Protein, Chez within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
Y:F201
b:0.0
occ:1.00
|
F3
|
Y:BEF201
|
0.0
|
0.0
|
1.0
|
BE
|
Y:BEF201
|
1.5
|
0.4
|
1.0
|
F2
|
Y:BEF201
|
2.4
|
0.2
|
1.0
|
F1
|
Y:BEF201
|
2.4
|
0.1
|
1.0
|
OD1
|
Y:ASP57
|
2.5
|
0.2
|
1.0
|
N
|
Y:ALA88
|
2.5
|
0.1
|
1.0
|
CB
|
Y:ALA88
|
3.0
|
0.6
|
1.0
|
C
|
Y:THR87
|
3.2
|
0.1
|
1.0
|
CA
|
Y:ALA88
|
3.3
|
0.1
|
1.0
|
OG1
|
Y:THR87
|
3.3
|
0.7
|
1.0
|
CA
|
Y:THR87
|
3.4
|
0.5
|
1.0
|
OE1
|
Z:GLN147
|
3.5
|
88.2
|
1.0
|
CG
|
Y:ASP57
|
3.6
|
0.1
|
1.0
|
CB
|
Y:THR87
|
3.7
|
0.7
|
1.0
|
NE2
|
Z:GLN147
|
3.8
|
88.1
|
1.0
|
CE
|
Y:LYS109
|
3.9
|
76.6
|
1.0
|
NZ
|
Y:LYS109
|
3.9
|
75.4
|
1.0
|
CD
|
Y:LYS109
|
4.0
|
80.2
|
1.0
|
OD2
|
Y:ASP57
|
4.0
|
0.8
|
1.0
|
CD
|
Z:GLN147
|
4.1
|
90.7
|
1.0
|
MG
|
Y:MG301
|
4.3
|
84.2
|
1.0
|
O
|
Y:THR87
|
4.3
|
0.9
|
1.0
|
C
|
Y:ALA88
|
4.4
|
0.1
|
1.0
|
N
|
Y:GLU89
|
4.5
|
0.9
|
1.0
|
OD2
|
Z:ASP143
|
4.6
|
0.1
|
1.0
|
CG
|
Y:LYS109
|
4.7
|
87.4
|
1.0
|
N
|
Y:THR87
|
4.7
|
0.3
|
1.0
|
CB
|
Y:ASP57
|
4.8
|
0.1
|
1.0
|
N
|
Y:TRP58
|
4.9
|
0.0
|
1.0
|
O
|
Y:VAL86
|
5.0
|
0.2
|
1.0
|
|
Reference:
R.Zhao,
E.J.Collins,
R.B.Bourret,
R.E.Silversmith.
Structure and Catalytic Mechanism of the E. Coli Chemotaxis Phosphatase Chez. Nat.Struct.Biol. V. 9 570 2002.
ISSN: ISSN 1072-8368
PubMed: 12080332
Page generated: Wed Jul 31 11:44:59 2024
|