Iron in PDB 6etb: Aerobic S262Y Mutation of E. Coli Flrd Core
Protein crystallography data
The structure of Aerobic S262Y Mutation of E. Coli Flrd Core, PDB code: 6etb
was solved by
P.T.Borges,
C.V.Romao,
M.A.Carrondo,
M.Teixeira,
C.Frazao,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
75.76 /
1.91
|
Space group
|
I 1 2 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
89.383,
64.407,
147.254,
90.00,
91.09,
90.00
|
R / Rfree (%)
|
20 /
20
|
Iron Binding Sites:
The binding sites of Iron atom in the Aerobic S262Y Mutation of E. Coli Flrd Core
(pdb code 6etb). This binding sites where shown within
5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the
Aerobic S262Y Mutation of E. Coli Flrd Core, PDB code: 6etb:
Jump to Iron binding site number:
1;
2;
3;
4;
Iron binding site 1 out
of 4 in 6etb
Go back to
Iron Binding Sites List in 6etb
Iron binding site 1 out
of 4 in the Aerobic S262Y Mutation of E. Coli Flrd Core
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 1 of Aerobic S262Y Mutation of E. Coli Flrd Core within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe502
b:48.3
occ:1.00
|
O
|
A:O505
|
1.7
|
29.7
|
0.6
|
NE2
|
A:HIS84
|
2.2
|
62.3
|
1.0
|
NE2
|
A:HIS227
|
2.2
|
23.2
|
1.0
|
OD2
|
A:ASP83
|
2.3
|
60.2
|
1.0
|
O2
|
A:OXY504
|
2.5
|
46.9
|
1.0
|
OD1
|
A:ASP166
|
2.7
|
28.6
|
1.0
|
CD2
|
A:HIS227
|
2.7
|
22.3
|
1.0
|
CE1
|
A:HIS84
|
2.9
|
63.0
|
1.0
|
O1
|
A:OXY504
|
3.3
|
47.8
|
1.0
|
CG
|
A:ASP83
|
3.3
|
60.1
|
1.0
|
CD2
|
A:HIS84
|
3.3
|
61.3
|
1.0
|
CG
|
A:ASP166
|
3.4
|
25.1
|
1.0
|
CE1
|
A:HIS227
|
3.5
|
23.9
|
1.0
|
FE
|
A:FE503
|
3.6
|
38.9
|
1.0
|
OD2
|
A:ASP166
|
3.6
|
26.3
|
1.0
|
OD1
|
A:ASP83
|
3.6
|
59.4
|
1.0
|
OE1
|
A:GLU81
|
3.9
|
49.0
|
1.0
|
ND1
|
A:HIS84
|
4.0
|
62.7
|
1.0
|
CG
|
A:HIS227
|
4.0
|
21.9
|
1.0
|
CG
|
A:HIS84
|
4.3
|
61.5
|
1.0
|
ND1
|
A:HIS227
|
4.3
|
23.9
|
1.0
|
OG
|
A:SER226
|
4.4
|
16.9
|
1.0
|
OH
|
A:TYR194
|
4.4
|
30.2
|
1.0
|
O
|
A:HOH607
|
4.5
|
50.2
|
0.7
|
CB
|
A:ASP83
|
4.6
|
60.5
|
1.0
|
O
|
A:HOH784
|
4.7
|
45.4
|
1.0
|
CB
|
A:ASP166
|
4.8
|
20.9
|
1.0
|
CE1
|
A:HIS171
|
4.8
|
17.0
|
1.0
|
CD
|
A:GLU81
|
4.9
|
47.5
|
1.0
|
|
Iron binding site 2 out
of 4 in 6etb
Go back to
Iron Binding Sites List in 6etb
Iron binding site 2 out
of 4 in the Aerobic S262Y Mutation of E. Coli Flrd Core
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 2 of Aerobic S262Y Mutation of E. Coli Flrd Core within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe503
b:38.9
occ:1.00
|
OE1
|
A:GLU81
|
1.9
|
49.0
|
1.0
|
O
|
A:O505
|
2.1
|
29.7
|
0.6
|
OD2
|
A:ASP166
|
2.2
|
26.3
|
1.0
|
O
|
A:HOH628
|
2.5
|
53.0
|
1.0
|
NE2
|
A:HIS147
|
2.8
|
31.9
|
1.0
|
NE2
|
A:HIS79
|
2.9
|
29.2
|
1.0
|
CE1
|
A:HIS147
|
3.0
|
31.8
|
1.0
|
O
|
A:HOH607
|
3.0
|
50.2
|
0.7
|
CD
|
A:GLU81
|
3.0
|
47.5
|
1.0
|
O1
|
A:OXY504
|
3.1
|
47.8
|
1.0
|
CD2
|
A:HIS79
|
3.2
|
27.5
|
1.0
|
CG
|
A:ASP166
|
3.3
|
25.1
|
1.0
|
O2
|
A:OXY504
|
3.5
|
46.9
|
1.0
|
FE
|
A:FE502
|
3.6
|
48.3
|
1.0
|
OE2
|
A:GLU81
|
3.6
|
47.5
|
1.0
|
OD1
|
A:ASP166
|
3.8
|
28.6
|
1.0
|
CD2
|
A:HIS147
|
4.0
|
29.7
|
1.0
|
CE1
|
A:HIS79
|
4.1
|
28.9
|
1.0
|
NE2
|
A:HIS84
|
4.2
|
62.3
|
1.0
|
CG
|
A:GLU81
|
4.2
|
46.1
|
1.0
|
CB
|
A:GLU81
|
4.2
|
44.9
|
1.0
|
ND1
|
A:HIS147
|
4.2
|
30.1
|
1.0
|
CD2
|
A:HIS84
|
4.3
|
61.3
|
1.0
|
CB
|
A:ASP166
|
4.5
|
20.9
|
1.0
|
OD1
|
A:ASP83
|
4.5
|
59.4
|
1.0
|
CG
|
A:HIS79
|
4.6
|
25.4
|
1.0
|
OH
|
A:TYR194
|
4.7
|
30.2
|
1.0
|
CG
|
A:HIS147
|
4.8
|
28.4
|
1.0
|
O
|
A:HOH791
|
4.8
|
30.9
|
1.0
|
OD2
|
A:ASP83
|
4.8
|
60.2
|
1.0
|
ND1
|
A:HIS79
|
5.0
|
26.4
|
1.0
|
|
Iron binding site 3 out
of 4 in 6etb
Go back to
Iron Binding Sites List in 6etb
Iron binding site 3 out
of 4 in the Aerobic S262Y Mutation of E. Coli Flrd Core
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 3 of Aerobic S262Y Mutation of E. Coli Flrd Core within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe502
b:44.2
occ:1.00
|
O
|
B:O505
|
1.7
|
36.3
|
0.6
|
NE2
|
B:HIS84
|
2.2
|
56.0
|
1.0
|
NE2
|
B:HIS227
|
2.2
|
22.7
|
1.0
|
OD2
|
B:ASP83
|
2.3
|
59.2
|
1.0
|
OD1
|
B:ASP166
|
2.5
|
28.5
|
1.0
|
O1
|
B:OXY504
|
2.7
|
51.1
|
1.0
|
CD2
|
B:HIS227
|
2.7
|
23.9
|
1.0
|
CE1
|
B:HIS84
|
2.7
|
57.4
|
1.0
|
CG
|
B:ASP83
|
3.3
|
58.1
|
1.0
|
CG
|
B:ASP166
|
3.3
|
25.9
|
1.0
|
O2
|
B:OXY504
|
3.3
|
55.1
|
1.0
|
CD2
|
B:HIS84
|
3.4
|
55.8
|
1.0
|
O
|
B:HOH660
|
3.5
|
48.4
|
1.0
|
CE1
|
B:HIS227
|
3.5
|
23.7
|
1.0
|
OD2
|
B:ASP166
|
3.5
|
26.5
|
1.0
|
FE
|
B:FE503
|
3.6
|
40.1
|
1.0
|
OD1
|
B:ASP83
|
3.7
|
56.9
|
1.0
|
ND1
|
B:HIS84
|
3.9
|
58.0
|
1.0
|
CG
|
B:HIS227
|
4.0
|
23.6
|
1.0
|
OE1
|
B:GLU81
|
4.1
|
51.6
|
1.0
|
CG
|
B:HIS84
|
4.3
|
57.7
|
1.0
|
OG
|
B:SER226
|
4.3
|
17.9
|
1.0
|
ND1
|
B:HIS227
|
4.3
|
24.6
|
1.0
|
OH
|
B:TYR194
|
4.4
|
29.6
|
1.0
|
CB
|
B:ASP83
|
4.6
|
58.3
|
1.0
|
CB
|
B:ASP166
|
4.7
|
23.8
|
1.0
|
O
|
B:HOH604
|
4.9
|
47.6
|
1.0
|
CE1
|
B:HIS171
|
4.9
|
18.4
|
1.0
|
CD
|
B:GLU81
|
5.0
|
49.5
|
1.0
|
|
Iron binding site 4 out
of 4 in 6etb
Go back to
Iron Binding Sites List in 6etb
Iron binding site 4 out
of 4 in the Aerobic S262Y Mutation of E. Coli Flrd Core
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 4 of Aerobic S262Y Mutation of E. Coli Flrd Core within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe503
b:40.1
occ:1.00
|
OE1
|
B:GLU81
|
1.9
|
51.6
|
1.0
|
O
|
B:O505
|
2.1
|
36.3
|
0.6
|
OD2
|
B:ASP166
|
2.1
|
26.5
|
1.0
|
NE2
|
B:HIS147
|
2.6
|
39.6
|
1.0
|
NE2
|
B:HIS79
|
2.7
|
30.8
|
1.0
|
CE1
|
B:HIS147
|
2.7
|
38.7
|
1.0
|
CD
|
B:GLU81
|
3.1
|
49.5
|
1.0
|
CD2
|
B:HIS79
|
3.1
|
29.4
|
1.0
|
O2
|
B:OXY504
|
3.1
|
55.1
|
1.0
|
CG
|
B:ASP166
|
3.2
|
25.9
|
1.0
|
O
|
B:HOH604
|
3.2
|
47.6
|
1.0
|
FE
|
B:FE502
|
3.6
|
44.2
|
1.0
|
OE2
|
B:GLU81
|
3.7
|
49.6
|
1.0
|
OD1
|
B:ASP166
|
3.7
|
28.5
|
1.0
|
O1
|
B:OXY504
|
3.7
|
51.1
|
1.0
|
CD2
|
B:HIS147
|
3.9
|
38.7
|
1.0
|
CE1
|
B:HIS79
|
3.9
|
29.6
|
1.0
|
ND1
|
B:HIS147
|
4.0
|
36.9
|
1.0
|
NE2
|
B:HIS84
|
4.0
|
56.0
|
1.0
|
CB
|
B:GLU81
|
4.2
|
44.7
|
1.0
|
CG
|
B:GLU81
|
4.2
|
46.8
|
1.0
|
CD2
|
B:HIS84
|
4.2
|
55.8
|
1.0
|
CB
|
B:ASP166
|
4.4
|
23.8
|
1.0
|
CG
|
B:HIS79
|
4.4
|
27.6
|
1.0
|
OD1
|
B:ASP83
|
4.6
|
56.9
|
1.0
|
CG
|
B:HIS147
|
4.6
|
36.6
|
1.0
|
O
|
B:HOH613
|
4.6
|
46.8
|
1.0
|
OH
|
B:TYR194
|
4.7
|
29.6
|
1.0
|
O
|
B:HOH660
|
4.8
|
48.4
|
1.0
|
ND1
|
B:HIS79
|
4.8
|
27.4
|
1.0
|
OD2
|
B:ASP83
|
4.8
|
59.2
|
1.0
|
|
Reference:
P.T.Borges,
C.V.Romao,
M.A.Carrondo,
M.Teixeira,
C.Frazao.
A Tyrosine Mutation in E. Coli Flavodiiron Protein Increases Radiation Sensitivity in the Crystal Structure To Be Published.
Page generated: Tue Aug 6 17:29:21 2024
|