Caesium in PDB 1i9d: Arsenate Reductase From E. Coli
Protein crystallography data
The structure of Arsenate Reductase From E. Coli, PDB code: 1i9d
was solved by
P.Martin,
B.F.Edwards,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
20.00 /
1.65
|
Space group
|
P 61 2 2
|
Cell size a, b, c (Å), α, β, γ (°)
|
86.726,
86.726,
116.170,
90.00,
90.00,
120.00
|
R / Rfree (%)
|
14 /
20.3
|
Caesium Binding Sites:
The binding sites of Caesium atom in the Arsenate Reductase From E. Coli
(pdb code 1i9d). This binding sites where shown within
5.0 Angstroms radius around Caesium atom.
In total 10 binding sites of Caesium where determined in the
Arsenate Reductase From E. Coli, PDB code: 1i9d:
Jump to Caesium binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
9;
10;
Caesium binding site 1 out
of 10 in 1i9d
Go back to
Caesium Binding Sites List in 1i9d
Caesium binding site 1 out
of 10 in the Arsenate Reductase From E. Coli
Mono view
Stereo pair view
|
A full contact list of Caesium with other atoms in the Cs binding
site number 1 of Arsenate Reductase From E. Coli within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cs602
b:24.8
occ:0.50
|
O
|
A:LEU116
|
3.1
|
24.6
|
1.0
|
O
|
A:LEU113
|
3.1
|
23.3
|
1.0
|
O
|
A:HOH625
|
3.1
|
25.8
|
1.0
|
O
|
A:ASP114
|
3.3
|
25.0
|
1.0
|
C
|
A:ASP114
|
3.8
|
24.4
|
1.0
|
O
|
A:HOH617
|
4.2
|
23.6
|
1.0
|
C
|
A:LEU116
|
4.2
|
21.5
|
1.0
|
C
|
A:LEU113
|
4.3
|
20.5
|
1.0
|
CA
|
A:ASP114
|
4.3
|
23.0
|
1.0
|
N
|
A:ILE115
|
4.5
|
21.9
|
1.0
|
CD1
|
A:LEU101
|
4.6
|
26.7
|
1.0
|
N
|
A:LEU116
|
4.6
|
23.7
|
1.0
|
N
|
A:ASP114
|
4.8
|
21.4
|
1.0
|
C
|
A:ILE115
|
4.9
|
23.0
|
1.0
|
CA
|
A:ILE115
|
5.0
|
23.9
|
1.0
|
CA
|
A:LEU116
|
5.0
|
23.0
|
1.0
|
|
Caesium binding site 2 out
of 10 in 1i9d
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Caesium Binding Sites List in 1i9d
Caesium binding site 2 out
of 10 in the Arsenate Reductase From E. Coli
Mono view
Stereo pair view
|
A full contact list of Caesium with other atoms in the Cs binding
site number 2 of Arsenate Reductase From E. Coli within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cs603
b:43.2
occ:0.40
|
O
|
A:HOH857
|
3.0
|
38.5
|
0.5
|
O
|
A:HOH627
|
3.2
|
27.2
|
1.0
|
O
|
A:HOH695
|
3.3
|
29.1
|
1.0
|
O
|
A:HOH739
|
3.7
|
51.9
|
1.0
|
OD2
|
A:ASP128
|
3.8
|
30.7
|
1.0
|
O
|
A:HOH616
|
4.4
|
24.2
|
1.0
|
CG
|
A:ASP128
|
4.5
|
27.1
|
1.0
|
OE2
|
A:GLU130
|
4.7
|
38.8
|
0.5
|
O4
|
A:SO4402
|
4.7
|
49.8
|
1.0
|
CB
|
A:ASP128
|
4.8
|
24.7
|
1.0
|
O1
|
A:SO4404
|
4.9
|
31.7
|
1.0
|
O1
|
A:SO4402
|
5.0
|
33.2
|
1.0
|
|
Caesium binding site 3 out
of 10 in 1i9d
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Caesium Binding Sites List in 1i9d
Caesium binding site 3 out
of 10 in the Arsenate Reductase From E. Coli
Mono view
Stereo pair view
|
A full contact list of Caesium with other atoms in the Cs binding
site number 3 of Arsenate Reductase From E. Coli within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cs604
b:41.6
occ:0.24
|
O
|
A:HOH905
|
2.7
|
40.0
|
0.5
|
O
|
A:PRO38
|
3.2
|
27.7
|
1.0
|
O
|
A:HOH651
|
3.2
|
27.0
|
1.0
|
OE1
|
A:GLU43
|
3.3
|
38.0
|
0.5
|
O
|
A:HOH751
|
3.4
|
42.0
|
1.0
|
O
|
A:HOH971
|
3.4
|
53.6
|
0.5
|
N
|
A:SER40
|
3.7
|
26.4
|
1.0
|
O
|
A:HOH967
|
3.8
|
46.7
|
0.5
|
C
|
A:PRO39
|
4.0
|
26.1
|
1.0
|
CA
|
A:PRO39
|
4.1
|
26.4
|
1.0
|
CD
|
A:GLU43
|
4.2
|
33.9
|
0.5
|
C
|
A:PRO38
|
4.2
|
25.0
|
1.0
|
O
|
A:HOH652
|
4.2
|
29.9
|
1.0
|
OE2
|
A:GLU43
|
4.3
|
37.5
|
0.5
|
CA
|
A:SER40
|
4.5
|
25.4
|
1.0
|
CB
|
A:SER40
|
4.5
|
28.2
|
1.0
|
N
|
A:PRO39
|
4.6
|
28.1
|
1.0
|
O
|
A:HOH736
|
4.8
|
39.6
|
1.0
|
O
|
A:PRO39
|
4.8
|
27.6
|
1.0
|
O
|
A:ASN37
|
5.0
|
28.1
|
1.0
|
|
Caesium binding site 4 out
of 10 in 1i9d
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Caesium Binding Sites List in 1i9d
Caesium binding site 4 out
of 10 in the Arsenate Reductase From E. Coli
Mono view
Stereo pair view
|
A full contact list of Caesium with other atoms in the Cs binding
site number 4 of Arsenate Reductase From E. Coli within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cs605
b:45.0
occ:0.19
|
O
|
A:HOH915
|
2.5
|
62.6
|
1.0
|
O
|
A:HOH879
|
2.9
|
58.2
|
1.0
|
O
|
A:HOH686
|
3.1
|
37.4
|
1.0
|
O
|
A:GLY26
|
3.1
|
28.0
|
1.0
|
OG1
|
A:THR27
|
3.4
|
30.0
|
1.0
|
O
|
A:HOH992
|
3.7
|
45.4
|
0.5
|
C
|
A:GLY26
|
3.9
|
25.9
|
1.0
|
O
|
A:HOH808
|
4.2
|
45.4
|
1.0
|
CA
|
A:THR27
|
4.4
|
25.0
|
1.0
|
OD2
|
A:ASP118
|
4.5
|
31.1
|
1.0
|
N
|
A:THR27
|
4.5
|
25.8
|
1.0
|
CB
|
A:THR27
|
4.5
|
27.6
|
1.0
|
O
|
A:HOH721
|
4.7
|
41.1
|
1.0
|
O
|
A:HOH830
|
4.8
|
46.7
|
1.0
|
CA
|
A:GLY26
|
4.8
|
26.4
|
1.0
|
O
|
A:HOH987
|
4.9
|
38.6
|
0.5
|
O
|
A:HOH924
|
4.9
|
53.4
|
0.5
|
|
Caesium binding site 5 out
of 10 in 1i9d
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Caesium Binding Sites List in 1i9d
Caesium binding site 5 out
of 10 in the Arsenate Reductase From E. Coli
Mono view
Stereo pair view
|
A full contact list of Caesium with other atoms in the Cs binding
site number 5 of Arsenate Reductase From E. Coli within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cs606
b:49.0
occ:0.21
|
CS
|
A:CS608
|
2.6
|
53.7
|
0.2
|
O
|
A:HOH717
|
3.1
|
33.8
|
1.0
|
O
|
A:HOH680
|
3.1
|
33.8
|
1.0
|
O
|
A:HOH973
|
3.1
|
47.3
|
0.5
|
OE2
|
A:GLU64
|
3.3
|
30.4
|
1.0
|
CD
|
A:GLU64
|
4.0
|
28.9
|
1.0
|
OE1
|
A:GLU64
|
4.2
|
30.4
|
1.0
|
O
|
A:HOH734
|
4.4
|
39.1
|
1.0
|
O
|
A:HOH771
|
4.4
|
41.4
|
1.0
|
O
|
A:HOH963
|
4.6
|
57.2
|
0.5
|
|
Caesium binding site 6 out
of 10 in 1i9d
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Caesium Binding Sites List in 1i9d
Caesium binding site 6 out
of 10 in the Arsenate Reductase From E. Coli
Mono view
Stereo pair view
|
A full contact list of Caesium with other atoms in the Cs binding
site number 6 of Arsenate Reductase From E. Coli within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cs607
b:51.1
occ:0.19
|
O
|
A:HOH782
|
2.3
|
47.5
|
1.0
|
O
|
A:HOH731
|
2.6
|
39.0
|
1.0
|
O
|
A:HOH811
|
2.6
|
61.8
|
1.0
|
O
|
A:HOH658
|
3.1
|
30.6
|
1.0
|
O
|
A:GLU135
|
3.2
|
38.3
|
1.0
|
O
|
A:GLN120
|
3.3
|
24.6
|
1.0
|
O
|
A:HOH807
|
3.6
|
43.2
|
0.5
|
O
|
A:LYS121
|
3.8
|
32.0
|
1.0
|
C
|
A:LYS121
|
3.8
|
24.6
|
1.0
|
N
|
A:GLY122
|
3.9
|
26.2
|
1.0
|
CA
|
A:GLY122
|
4.0
|
26.9
|
1.0
|
C
|
A:GLU135
|
4.3
|
32.3
|
1.0
|
N
|
A:GLY137
|
4.3
|
30.7
|
1.0
|
C
|
A:ALA136
|
4.3
|
36.0
|
1.0
|
C
|
A:GLN120
|
4.4
|
24.7
|
1.0
|
CA
|
A:GLY137
|
4.4
|
29.2
|
1.0
|
O
|
A:ALA136
|
4.5
|
37.6
|
1.0
|
CA
|
A:LYS121
|
4.5
|
23.9
|
1.0
|
C
|
A:GLY122
|
4.7
|
22.8
|
1.0
|
CA
|
A:ALA136
|
4.8
|
32.9
|
1.0
|
N
|
A:LYS121
|
4.9
|
23.6
|
1.0
|
OE1
|
A:GLU135
|
5.0
|
51.5
|
1.0
|
|
Caesium binding site 7 out
of 10 in 1i9d
Go back to
Caesium Binding Sites List in 1i9d
Caesium binding site 7 out
of 10 in the Arsenate Reductase From E. Coli
Mono view
Stereo pair view
|
A full contact list of Caesium with other atoms in the Cs binding
site number 7 of Arsenate Reductase From E. Coli within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cs608
b:53.7
occ:0.17
|
CS
|
A:CS606
|
2.6
|
49.0
|
0.2
|
O
|
A:HOH973
|
2.6
|
47.3
|
0.5
|
O
|
A:HOH733
|
2.8
|
44.3
|
1.0
|
O
|
A:HOH771
|
2.9
|
41.4
|
1.0
|
OE2
|
A:GLU64
|
3.1
|
30.4
|
1.0
|
O
|
A:HOH734
|
3.5
|
39.1
|
1.0
|
O
|
A:HOH680
|
3.7
|
33.8
|
1.0
|
O
|
A:HOH963
|
3.7
|
57.2
|
0.5
|
CD
|
A:GLU64
|
3.8
|
28.9
|
1.0
|
CB
|
A:GLU64
|
4.2
|
25.0
|
1.0
|
O
|
A:HOH674
|
4.3
|
44.4
|
1.0
|
CG
|
A:GLU64
|
4.4
|
25.8
|
1.0
|
O
|
A:HOH765
|
4.5
|
49.4
|
1.0
|
O
|
A:HOH802
|
4.5
|
44.7
|
0.5
|
OE1
|
A:GLU64
|
4.6
|
30.4
|
1.0
|
O
|
A:HOH653
|
4.8
|
32.7
|
1.0
|
O
|
A:HOH717
|
4.9
|
33.8
|
1.0
|
|
Caesium binding site 8 out
of 10 in 1i9d
Go back to
Caesium Binding Sites List in 1i9d
Caesium binding site 8 out
of 10 in the Arsenate Reductase From E. Coli
Mono view
Stereo pair view
|
A full contact list of Caesium with other atoms in the Cs binding
site number 8 of Arsenate Reductase From E. Coli within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cs609
b:39.5
occ:0.16
|
O
|
A:HOH677
|
2.7
|
28.7
|
1.0
|
OE1
|
A:GLU73
|
3.4
|
72.7
|
1.0
|
CA
|
A:GLY70
|
3.8
|
24.9
|
1.0
|
CD
|
A:GLU73
|
4.0
|
57.0
|
1.0
|
CG
|
A:GLU73
|
4.4
|
39.5
|
1.0
|
C
|
A:GLY70
|
4.8
|
22.7
|
1.0
|
O
|
A:GLY70
|
4.8
|
25.2
|
1.0
|
N
|
A:GLY70
|
4.8
|
24.1
|
1.0
|
OE2
|
A:GLU73
|
4.8
|
76.4
|
1.0
|
|
Caesium binding site 9 out
of 10 in 1i9d
Go back to
Caesium Binding Sites List in 1i9d
Caesium binding site 9 out
of 10 in the Arsenate Reductase From E. Coli
Mono view
Stereo pair view
|
A full contact list of Caesium with other atoms in the Cs binding
site number 9 of Arsenate Reductase From E. Coli within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cs610
b:0.2
occ:0.15
|
O
|
A:HOH789
|
3.3
|
53.5
|
1.0
|
O
|
A:ASN62
|
3.4
|
32.9
|
1.0
|
CB
|
A:ASN62
|
4.0
|
45.2
|
1.0
|
O
|
A:HOH816
|
4.3
|
52.3
|
1.0
|
C
|
A:ASN62
|
4.4
|
29.4
|
1.0
|
CA
|
A:ASN62
|
4.8
|
31.9
|
1.0
|
CG
|
A:ASN62
|
4.9
|
48.3
|
1.0
|
|
Caesium binding site 10 out
of 10 in 1i9d
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Caesium Binding Sites List in 1i9d
Caesium binding site 10 out
of 10 in the Arsenate Reductase From E. Coli
Mono view
Stereo pair view
|
A full contact list of Caesium with other atoms in the Cs binding
site number 10 of Arsenate Reductase From E. Coli within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cs611
b:61.1
occ:0.20
|
OG1
|
A:THR30
|
2.7
|
30.3
|
1.0
|
O
|
A:HOH643
|
2.7
|
29.7
|
1.0
|
O
|
A:HOH875
|
3.0
|
44.1
|
0.5
|
O
|
A:ILE4
|
3.2
|
25.1
|
1.0
|
O
|
A:HOH979
|
3.5
|
51.7
|
0.5
|
N
|
A:ILE4
|
3.6
|
25.3
|
1.0
|
ND2
|
A:ASN3
|
3.7
|
58.5
|
1.0
|
N
|
A:THR30
|
3.7
|
24.0
|
1.0
|
CB
|
A:THR30
|
3.8
|
30.6
|
1.0
|
CA
|
A:ASN3
|
4.1
|
32.7
|
1.0
|
C
|
A:ILE4
|
4.1
|
23.8
|
1.0
|
C
|
A:ASN3
|
4.3
|
27.5
|
1.0
|
CA
|
A:THR30
|
4.3
|
26.1
|
1.0
|
O
|
A:HOH882
|
4.5
|
48.9
|
0.5
|
CA
|
A:ILE4
|
4.5
|
23.3
|
1.0
|
C
|
A:PRO29
|
4.6
|
25.4
|
1.0
|
O
|
A:HOH855
|
4.7
|
36.9
|
0.5
|
CG
|
A:ASN3
|
4.7
|
55.8
|
1.0
|
CA
|
A:PRO29
|
4.8
|
23.5
|
1.0
|
O
|
A:GLU28
|
4.8
|
28.1
|
1.0
|
O
|
A:HOH861
|
4.9
|
51.8
|
0.5
|
CB
|
A:ASN3
|
4.9
|
40.4
|
1.0
|
OG1
|
A:THR5
|
5.0
|
27.6
|
1.0
|
|
Reference:
P.Martin,
S.Demel,
J.Shi,
T.Gladysheva,
D.L.Gatti,
B.P.Rosen,
B.F.Edwards.
Insights Into the Structure, Solvation, and Mechanism of Arsc Arsenate Reductase, A Novel Arsenic Detoxification Enzyme. Structure V. 9 1071 2001.
ISSN: ISSN 0969-2126
PubMed: 11709171
DOI: 10.1016/S0969-2126(01)00672-4
Page generated: Tue Jul 30 20:09:00 2024
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