Iron in PDB 7p46: Crystal Structure of Xanthomonas Campestris Tryptophan 2,3-Dioxygenase (Tdo)
Enzymatic activity of Crystal Structure of Xanthomonas Campestris Tryptophan 2,3-Dioxygenase (Tdo)
All present enzymatic activity of Crystal Structure of Xanthomonas Campestris Tryptophan 2,3-Dioxygenase (Tdo):
1.13.11.11;
Protein crystallography data
The structure of Crystal Structure of Xanthomonas Campestris Tryptophan 2,3-Dioxygenase (Tdo), PDB code: 7p46
was solved by
H.Kwon,
J.Basran,
E.S.Booth,
L.P.Campbell,
S.J.Thackray,
P.C.E.Moody,
C.G.Mowat,
E.L.Raven,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
|
Resolution Low / High (Å)
|
89.78 /
1.70
|
|
Space group
|
P 1 21 1
|
|
Cell size a, b, c (Å), α, β, γ (°)
|
78.095,
117.752,
138.819,
90,
95.52,
90
|
|
R / Rfree (%)
|
14.9 /
18.5
|
Iron Binding Sites:
The binding sites of Iron atom in the Crystal Structure of Xanthomonas Campestris Tryptophan 2,3-Dioxygenase (Tdo)
(pdb code 7p46). This binding sites where shown within
5.0 Angstroms radius around Iron atom.
In total 8 binding sites of Iron where determined in the
Crystal Structure of Xanthomonas Campestris Tryptophan 2,3-Dioxygenase (Tdo), PDB code: 7p46:
Jump to Iron binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
Iron binding site 1 out
of 8 in 7p46
Go back to
Iron Binding Sites List in 7p46
Iron binding site 1 out
of 8 in the Crystal Structure of Xanthomonas Campestris Tryptophan 2,3-Dioxygenase (Tdo)
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 1 of Crystal Structure of Xanthomonas Campestris Tryptophan 2,3-Dioxygenase (Tdo) within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe301
b:10.8
occ:1.00
|
FE
|
A:HEM301
|
0.0
|
10.8
|
1.0
|
|
C
|
A:CYN302
|
1.7
|
8.2
|
1.0
|
|
ND
|
A:HEM301
|
2.0
|
10.5
|
1.0
|
|
NA
|
A:HEM301
|
2.0
|
9.3
|
1.0
|
|
NC
|
A:HEM301
|
2.0
|
9.8
|
1.0
|
|
NB
|
A:HEM301
|
2.0
|
10.6
|
1.0
|
|
NE2
|
A:HIS240
|
2.0
|
11.3
|
1.0
|
|
C4D
|
A:HEM301
|
3.0
|
10.2
|
1.0
|
|
N
|
A:CYN302
|
3.0
|
9.4
|
1.0
|
|
C1D
|
A:HEM301
|
3.0
|
9.3
|
1.0
|
|
C1A
|
A:HEM301
|
3.0
|
10.9
|
1.0
|
|
C1B
|
A:HEM301
|
3.0
|
10.6
|
1.0
|
|
CE1
|
A:HIS240
|
3.0
|
11.5
|
1.0
|
|
C1C
|
A:HEM301
|
3.0
|
11.6
|
1.0
|
|
C4A
|
A:HEM301
|
3.0
|
10.4
|
1.0
|
|
C4C
|
A:HEM301
|
3.0
|
10.7
|
1.0
|
|
C4B
|
A:HEM301
|
3.0
|
11.0
|
1.0
|
|
CD2
|
A:HIS240
|
3.1
|
12.3
|
1.0
|
|
CHB
|
A:HEM301
|
3.4
|
11.1
|
1.0
|
|
CHA
|
A:HEM301
|
3.4
|
10.6
|
1.0
|
|
CHC
|
A:HEM301
|
3.4
|
12.4
|
1.0
|
|
CHD
|
A:HEM301
|
3.5
|
11.0
|
1.0
|
|
ND1
|
A:HIS240
|
4.2
|
11.9
|
1.0
|
|
C2C
|
A:HEM301
|
4.2
|
10.6
|
1.0
|
|
CG
|
A:HIS240
|
4.2
|
11.6
|
1.0
|
|
C3D
|
A:HEM301
|
4.2
|
9.8
|
1.0
|
|
C3A
|
A:HEM301
|
4.2
|
11.2
|
1.0
|
|
C2A
|
A:HEM301
|
4.3
|
10.7
|
1.0
|
|
C2D
|
A:HEM301
|
4.3
|
10.7
|
1.0
|
|
C3C
|
A:HEM301
|
4.3
|
11.4
|
1.0
|
|
C2B
|
A:HEM301
|
4.3
|
12.6
|
1.0
|
|
C3B
|
A:HEM301
|
4.3
|
12.3
|
1.0
|
|
O2
|
A:KYN303
|
4.4
|
11.7
|
1.0
|
|
N
|
A:KYN303
|
4.7
|
11.8
|
1.0
|
|
CG2
|
A:VAL244
|
4.8
|
12.5
|
1.0
|
|
N1
|
A:KYN303
|
4.8
|
12.4
|
1.0
|
|
Iron binding site 2 out
of 8 in 7p46
Go back to
Iron Binding Sites List in 7p46
Iron binding site 2 out
of 8 in the Crystal Structure of Xanthomonas Campestris Tryptophan 2,3-Dioxygenase (Tdo)
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 2 of Crystal Structure of Xanthomonas Campestris Tryptophan 2,3-Dioxygenase (Tdo) within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe301
b:9.4
occ:1.00
|
FE
|
B:HEM301
|
0.0
|
9.4
|
1.0
|
|
C
|
B:CYN302
|
1.8
|
6.1
|
1.0
|
|
ND
|
B:HEM301
|
1.9
|
8.8
|
1.0
|
|
NA
|
B:HEM301
|
2.0
|
7.8
|
1.0
|
|
NC
|
B:HEM301
|
2.0
|
8.5
|
1.0
|
|
NE2
|
B:HIS240
|
2.0
|
8.6
|
1.0
|
|
NB
|
B:HEM301
|
2.0
|
8.9
|
1.0
|
|
C1D
|
B:HEM301
|
2.9
|
8.4
|
1.0
|
|
CE1
|
B:HIS240
|
3.0
|
10.6
|
1.0
|
|
C4D
|
B:HEM301
|
3.0
|
8.5
|
1.0
|
|
C1A
|
B:HEM301
|
3.0
|
9.2
|
1.0
|
|
C4A
|
B:HEM301
|
3.0
|
9.3
|
1.0
|
|
C1C
|
B:HEM301
|
3.0
|
9.4
|
1.0
|
|
C4B
|
B:HEM301
|
3.0
|
8.4
|
1.0
|
|
C1B
|
B:HEM301
|
3.0
|
8.5
|
1.0
|
|
C4C
|
B:HEM301
|
3.0
|
9.5
|
1.0
|
|
N
|
B:CYN302
|
3.1
|
8.9
|
1.0
|
|
CD2
|
B:HIS240
|
3.2
|
9.8
|
1.0
|
|
CHD
|
B:HEM301
|
3.4
|
8.6
|
1.0
|
|
CHB
|
B:HEM301
|
3.4
|
9.2
|
1.0
|
|
CHA
|
B:HEM301
|
3.4
|
9.0
|
1.0
|
|
CHC
|
B:HEM301
|
3.5
|
8.8
|
1.0
|
|
ND1
|
B:HIS240
|
4.1
|
10.8
|
1.0
|
|
C3A
|
B:HEM301
|
4.2
|
9.2
|
1.0
|
|
C2C
|
B:HEM301
|
4.2
|
8.9
|
1.0
|
|
C3C
|
B:HEM301
|
4.2
|
9.3
|
1.0
|
|
C2A
|
B:HEM301
|
4.2
|
9.1
|
1.0
|
|
C2D
|
B:HEM301
|
4.2
|
8.8
|
1.0
|
|
C2B
|
B:HEM301
|
4.2
|
8.6
|
1.0
|
|
CG
|
B:HIS240
|
4.3
|
10.0
|
1.0
|
|
C3D
|
B:HEM301
|
4.3
|
8.8
|
1.0
|
|
C3B
|
B:HEM301
|
4.3
|
9.0
|
1.0
|
|
O2
|
B:KYN303
|
4.3
|
10.0
|
1.0
|
|
N1
|
B:KYN303
|
4.7
|
12.0
|
1.0
|
|
CG2
|
B:VAL244
|
4.7
|
11.6
|
1.0
|
|
N
|
B:KYN303
|
4.7
|
10.4
|
1.0
|
|
N
|
B:GLY125
|
4.9
|
10.8
|
1.0
|
|
CA
|
B:GLY125
|
5.0
|
10.9
|
1.0
|
|
C1
|
B:KYN303
|
5.0
|
9.3
|
1.0
|
|
Iron binding site 3 out
of 8 in 7p46
Go back to
Iron Binding Sites List in 7p46
Iron binding site 3 out
of 8 in the Crystal Structure of Xanthomonas Campestris Tryptophan 2,3-Dioxygenase (Tdo)
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 3 of Crystal Structure of Xanthomonas Campestris Tryptophan 2,3-Dioxygenase (Tdo) within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Fe301
b:16.6
occ:1.00
|
FE
|
C:HEM301
|
0.0
|
16.6
|
1.0
|
|
ND
|
C:HEM301
|
1.9
|
15.8
|
1.0
|
|
C
|
C:CYN302
|
2.0
|
15.7
|
1.0
|
|
NA
|
C:HEM301
|
2.0
|
14.9
|
1.0
|
|
NB
|
C:HEM301
|
2.0
|
15.7
|
1.0
|
|
NC
|
C:HEM301
|
2.1
|
14.5
|
1.0
|
|
NE2
|
C:HIS240
|
2.1
|
17.3
|
1.0
|
|
C4D
|
C:HEM301
|
2.9
|
16.6
|
1.0
|
|
C1A
|
C:HEM301
|
3.0
|
16.6
|
1.0
|
|
C1D
|
C:HEM301
|
3.0
|
16.0
|
1.0
|
|
CE1
|
C:HIS240
|
3.0
|
19.2
|
1.0
|
|
C1C
|
C:HEM301
|
3.0
|
14.8
|
1.0
|
|
C4A
|
C:HEM301
|
3.0
|
16.5
|
1.0
|
|
C1B
|
C:HEM301
|
3.0
|
14.9
|
1.0
|
|
C4B
|
C:HEM301
|
3.1
|
14.7
|
1.0
|
|
C4C
|
C:HEM301
|
3.1
|
15.5
|
1.0
|
|
CD2
|
C:HIS240
|
3.1
|
17.6
|
1.0
|
|
N
|
C:CYN302
|
3.1
|
20.4
|
1.0
|
|
CHA
|
C:HEM301
|
3.4
|
16.9
|
1.0
|
|
CHB
|
C:HEM301
|
3.4
|
16.2
|
1.0
|
|
CHC
|
C:HEM301
|
3.5
|
14.7
|
1.0
|
|
CHD
|
C:HEM301
|
3.5
|
16.0
|
1.0
|
|
ND1
|
C:HIS240
|
4.2
|
17.6
|
1.0
|
|
C2C
|
C:HEM301
|
4.2
|
14.0
|
1.0
|
|
C3D
|
C:HEM301
|
4.2
|
16.6
|
1.0
|
|
C2A
|
C:HEM301
|
4.2
|
16.6
|
1.0
|
|
CG
|
C:HIS240
|
4.2
|
15.6
|
1.0
|
|
C2D
|
C:HEM301
|
4.2
|
16.5
|
1.0
|
|
C3A
|
C:HEM301
|
4.2
|
16.1
|
1.0
|
|
C3C
|
C:HEM301
|
4.2
|
15.0
|
1.0
|
|
C2B
|
C:HEM301
|
4.3
|
14.8
|
1.0
|
|
O2
|
C:KYN303
|
4.3
|
19.8
|
1.0
|
|
C3B
|
C:HEM301
|
4.3
|
14.9
|
1.0
|
|
N1
|
C:KYN303
|
4.7
|
17.6
|
1.0
|
|
CG2
|
C:VAL244
|
4.7
|
16.5
|
1.0
|
|
N
|
C:KYN303
|
4.7
|
16.6
|
1.0
|
|
N
|
C:GLY125
|
4.9
|
19.5
|
1.0
|
|
C1
|
C:KYN303
|
4.9
|
19.0
|
1.0
|
|
Iron binding site 4 out
of 8 in 7p46
Go back to
Iron Binding Sites List in 7p46
Iron binding site 4 out
of 8 in the Crystal Structure of Xanthomonas Campestris Tryptophan 2,3-Dioxygenase (Tdo)
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 4 of Crystal Structure of Xanthomonas Campestris Tryptophan 2,3-Dioxygenase (Tdo) within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Fe301
b:15.8
occ:1.00
|
FE
|
D:HEM301
|
0.0
|
15.8
|
1.0
|
|
ND
|
D:HEM301
|
1.9
|
12.6
|
1.0
|
|
NB
|
D:HEM301
|
2.0
|
13.4
|
1.0
|
|
NA
|
D:HEM301
|
2.0
|
14.3
|
1.0
|
|
NC
|
D:HEM301
|
2.0
|
14.0
|
1.0
|
|
C
|
D:CYN302
|
2.1
|
12.3
|
1.0
|
|
NE2
|
D:HIS240
|
2.1
|
12.7
|
1.0
|
|
C1D
|
D:HEM301
|
2.9
|
14.2
|
1.0
|
|
C4B
|
D:HEM301
|
3.0
|
14.5
|
1.0
|
|
CE1
|
D:HIS240
|
3.0
|
16.2
|
1.0
|
|
C4D
|
D:HEM301
|
3.0
|
12.8
|
1.0
|
|
C1A
|
D:HEM301
|
3.0
|
13.8
|
1.0
|
|
C4C
|
D:HEM301
|
3.0
|
14.1
|
1.0
|
|
C4A
|
D:HEM301
|
3.0
|
13.7
|
1.0
|
|
C1B
|
D:HEM301
|
3.0
|
13.4
|
1.0
|
|
C1C
|
D:HEM301
|
3.0
|
14.0
|
1.0
|
|
CD2
|
D:HIS240
|
3.1
|
15.3
|
1.0
|
|
N
|
D:CYN302
|
3.3
|
20.2
|
1.0
|
|
CHD
|
D:HEM301
|
3.4
|
13.7
|
1.0
|
|
CHC
|
D:HEM301
|
3.4
|
15.5
|
1.0
|
|
CHB
|
D:HEM301
|
3.4
|
14.4
|
1.0
|
|
CHA
|
D:HEM301
|
3.5
|
14.0
|
1.0
|
|
ND1
|
D:HIS240
|
4.1
|
15.8
|
1.0
|
|
C3A
|
D:HEM301
|
4.2
|
13.9
|
1.0
|
|
C2D
|
D:HEM301
|
4.2
|
14.3
|
1.0
|
|
C2A
|
D:HEM301
|
4.2
|
15.0
|
1.0
|
|
C2B
|
D:HEM301
|
4.2
|
13.4
|
1.0
|
|
C3B
|
D:HEM301
|
4.2
|
14.3
|
1.0
|
|
C3D
|
D:HEM301
|
4.2
|
15.1
|
1.0
|
|
C3C
|
D:HEM301
|
4.2
|
14.2
|
1.0
|
|
CG
|
D:HIS240
|
4.2
|
14.1
|
1.0
|
|
C2C
|
D:HEM301
|
4.2
|
13.7
|
1.0
|
|
O2
|
D:KYN303
|
4.4
|
18.7
|
1.0
|
|
N1
|
D:KYN303
|
4.7
|
18.1
|
1.0
|
|
CG2
|
D:VAL244
|
4.7
|
15.0
|
1.0
|
|
N
|
D:KYN303
|
4.7
|
15.5
|
1.0
|
|
N
|
D:GLY125
|
4.9
|
20.0
|
1.0
|
|
CA
|
D:GLY125
|
4.9
|
17.2
|
1.0
|
|
Iron binding site 5 out
of 8 in 7p46
Go back to
Iron Binding Sites List in 7p46
Iron binding site 5 out
of 8 in the Crystal Structure of Xanthomonas Campestris Tryptophan 2,3-Dioxygenase (Tdo)
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 5 of Crystal Structure of Xanthomonas Campestris Tryptophan 2,3-Dioxygenase (Tdo) within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Fe301
b:26.9
occ:1.00
|
FE
|
E:HEM301
|
0.0
|
26.9
|
1.0
|
|
ND
|
E:HEM301
|
2.0
|
24.4
|
1.0
|
|
NA
|
E:HEM301
|
2.0
|
27.5
|
1.0
|
|
NC
|
E:HEM301
|
2.0
|
27.0
|
1.0
|
|
NB
|
E:HEM301
|
2.1
|
24.2
|
1.0
|
|
NE2
|
E:HIS240
|
2.2
|
24.2
|
1.0
|
|
O
|
E:HOH538
|
2.5
|
29.7
|
1.0
|
|
C4D
|
E:HEM301
|
3.0
|
24.6
|
1.0
|
|
C1D
|
E:HEM301
|
3.0
|
23.9
|
1.0
|
|
C4B
|
E:HEM301
|
3.0
|
25.7
|
1.0
|
|
C1A
|
E:HEM301
|
3.0
|
26.1
|
1.0
|
|
C4A
|
E:HEM301
|
3.0
|
28.1
|
1.0
|
|
C1C
|
E:HEM301
|
3.1
|
26.3
|
1.0
|
|
C4C
|
E:HEM301
|
3.1
|
28.9
|
1.0
|
|
C1B
|
E:HEM301
|
3.1
|
25.9
|
1.0
|
|
CE1
|
E:HIS240
|
3.1
|
28.1
|
1.0
|
|
CD2
|
E:HIS240
|
3.2
|
25.1
|
1.0
|
|
CHC
|
E:HEM301
|
3.4
|
26.0
|
1.0
|
|
CHA
|
E:HEM301
|
3.4
|
27.2
|
1.0
|
|
CHD
|
E:HEM301
|
3.4
|
27.1
|
1.0
|
|
CHB
|
E:HEM301
|
3.5
|
27.5
|
1.0
|
|
O2
|
E:KYN302
|
4.2
|
31.5
|
1.0
|
|
C2D
|
E:HEM301
|
4.2
|
24.8
|
1.0
|
|
C3A
|
E:HEM301
|
4.3
|
29.1
|
1.0
|
|
C2C
|
E:HEM301
|
4.3
|
28.2
|
1.0
|
|
C3D
|
E:HEM301
|
4.3
|
26.5
|
1.0
|
|
C2A
|
E:HEM301
|
4.3
|
27.0
|
1.0
|
|
ND1
|
E:HIS240
|
4.3
|
24.3
|
1.0
|
|
C2B
|
E:HEM301
|
4.3
|
25.6
|
1.0
|
|
C3C
|
E:HEM301
|
4.3
|
28.9
|
1.0
|
|
C3B
|
E:HEM301
|
4.3
|
25.6
|
1.0
|
|
CG
|
E:HIS240
|
4.3
|
22.4
|
1.0
|
|
N1
|
E:KYN302
|
4.6
|
27.1
|
1.0
|
|
N
|
E:KYN302
|
4.7
|
33.4
|
1.0
|
|
CG2
|
E:VAL244
|
4.7
|
27.7
|
1.0
|
|
N
|
E:GLY125
|
4.9
|
31.6
|
1.0
|
|
C1
|
E:KYN302
|
5.0
|
29.1
|
1.0
|
|
CA
|
E:GLY125
|
5.0
|
31.7
|
1.0
|
|
Iron binding site 6 out
of 8 in 7p46
Go back to
Iron Binding Sites List in 7p46
Iron binding site 6 out
of 8 in the Crystal Structure of Xanthomonas Campestris Tryptophan 2,3-Dioxygenase (Tdo)
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 6 of Crystal Structure of Xanthomonas Campestris Tryptophan 2,3-Dioxygenase (Tdo) within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
F:Fe301
b:20.1
occ:1.00
|
FE
|
F:HEM301
|
0.0
|
20.1
|
1.0
|
|
C
|
F:CYN302
|
1.9
|
17.9
|
1.0
|
|
ND
|
F:HEM301
|
2.0
|
18.1
|
1.0
|
|
NA
|
F:HEM301
|
2.0
|
19.4
|
1.0
|
|
NC
|
F:HEM301
|
2.0
|
18.1
|
1.0
|
|
NB
|
F:HEM301
|
2.1
|
17.5
|
1.0
|
|
NE2
|
F:HIS240
|
2.1
|
19.4
|
1.0
|
|
C1D
|
F:HEM301
|
3.0
|
20.2
|
1.0
|
|
C4D
|
F:HEM301
|
3.0
|
21.5
|
1.0
|
|
C4B
|
F:HEM301
|
3.0
|
19.3
|
1.0
|
|
CE1
|
F:HIS240
|
3.0
|
23.0
|
1.0
|
|
C1A
|
F:HEM301
|
3.0
|
21.3
|
1.0
|
|
C4C
|
F:HEM301
|
3.0
|
21.1
|
1.0
|
|
C4A
|
F:HEM301
|
3.1
|
22.2
|
1.0
|
|
C1C
|
F:HEM301
|
3.1
|
19.5
|
1.0
|
|
C1B
|
F:HEM301
|
3.1
|
20.6
|
1.0
|
|
N
|
F:CYN302
|
3.2
|
19.9
|
1.0
|
|
CD2
|
F:HIS240
|
3.2
|
22.8
|
1.0
|
|
CHD
|
F:HEM301
|
3.4
|
21.0
|
1.0
|
|
CHC
|
F:HEM301
|
3.4
|
20.0
|
1.0
|
|
CHA
|
F:HEM301
|
3.5
|
20.9
|
1.0
|
|
CHB
|
F:HEM301
|
3.5
|
20.2
|
1.0
|
|
ND1
|
F:HIS240
|
4.2
|
21.7
|
1.0
|
|
C2D
|
F:HEM301
|
4.2
|
20.8
|
1.0
|
|
C3D
|
F:HEM301
|
4.2
|
22.8
|
1.0
|
|
C2A
|
F:HEM301
|
4.2
|
21.2
|
1.0
|
|
C3A
|
F:HEM301
|
4.3
|
22.1
|
1.0
|
|
C3B
|
F:HEM301
|
4.3
|
17.7
|
1.0
|
|
C2B
|
F:HEM301
|
4.3
|
20.0
|
1.0
|
|
C2C
|
F:HEM301
|
4.3
|
20.3
|
1.0
|
|
C3C
|
F:HEM301
|
4.3
|
21.2
|
1.0
|
|
CG
|
F:HIS240
|
4.3
|
19.3
|
1.0
|
|
O2
|
F:KYN303
|
4.4
|
23.8
|
1.0
|
|
CG2
|
F:VAL244
|
4.7
|
21.4
|
1.0
|
|
N1
|
F:KYN303
|
4.8
|
23.1
|
1.0
|
|
N
|
F:KYN303
|
4.8
|
21.7
|
1.0
|
|
N
|
F:GLY125
|
4.8
|
24.1
|
1.0
|
|
CA
|
F:GLY125
|
4.9
|
23.7
|
1.0
|
|
C1
|
F:KYN303
|
5.0
|
22.0
|
1.0
|
|
Iron binding site 7 out
of 8 in 7p46
Go back to
Iron Binding Sites List in 7p46
Iron binding site 7 out
of 8 in the Crystal Structure of Xanthomonas Campestris Tryptophan 2,3-Dioxygenase (Tdo)
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 7 of Crystal Structure of Xanthomonas Campestris Tryptophan 2,3-Dioxygenase (Tdo) within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
G:Fe301
b:25.2
occ:1.00
|
FE
|
G:HEM301
|
0.0
|
25.2
|
1.0
|
|
ND
|
G:HEM301
|
1.9
|
21.9
|
1.0
|
|
NA
|
G:HEM301
|
2.0
|
20.9
|
1.0
|
|
NB
|
G:HEM301
|
2.1
|
23.0
|
1.0
|
|
NC
|
G:HEM301
|
2.1
|
23.1
|
1.0
|
|
NE2
|
G:HIS240
|
2.2
|
21.3
|
1.0
|
|
O
|
G:HOH495
|
2.6
|
28.4
|
1.0
|
|
C4D
|
G:HEM301
|
2.9
|
22.6
|
1.0
|
|
C1D
|
G:HEM301
|
3.0
|
23.2
|
1.0
|
|
C1A
|
G:HEM301
|
3.0
|
24.8
|
1.0
|
|
C4B
|
G:HEM301
|
3.0
|
24.0
|
1.0
|
|
C4A
|
G:HEM301
|
3.0
|
23.9
|
1.0
|
|
C1B
|
G:HEM301
|
3.0
|
25.9
|
1.0
|
|
C4C
|
G:HEM301
|
3.1
|
24.9
|
1.0
|
|
C1C
|
G:HEM301
|
3.1
|
24.7
|
1.0
|
|
CE1
|
G:HIS240
|
3.1
|
23.8
|
1.0
|
|
CD2
|
G:HIS240
|
3.2
|
24.4
|
1.0
|
|
CHA
|
G:HEM301
|
3.4
|
23.4
|
1.0
|
|
CHD
|
G:HEM301
|
3.4
|
24.0
|
1.0
|
|
CHC
|
G:HEM301
|
3.5
|
23.9
|
1.0
|
|
CHB
|
G:HEM301
|
3.5
|
23.6
|
1.0
|
|
C2A
|
G:HEM301
|
4.2
|
23.6
|
1.0
|
|
C3A
|
G:HEM301
|
4.2
|
23.3
|
1.0
|
|
C3D
|
G:HEM301
|
4.2
|
23.6
|
1.0
|
|
C2D
|
G:HEM301
|
4.2
|
23.0
|
1.0
|
|
C2B
|
G:HEM301
|
4.3
|
23.8
|
1.0
|
|
ND1
|
G:HIS240
|
4.3
|
23.5
|
1.0
|
|
C3B
|
G:HEM301
|
4.3
|
23.1
|
1.0
|
|
C3C
|
G:HEM301
|
4.3
|
27.7
|
1.0
|
|
C2C
|
G:HEM301
|
4.3
|
25.1
|
1.0
|
|
CG
|
G:HIS240
|
4.3
|
21.9
|
1.0
|
|
O2
|
G:KYN302
|
4.3
|
29.1
|
1.0
|
|
N1
|
G:KYN302
|
4.6
|
26.6
|
1.0
|
|
N
|
G:KYN302
|
4.7
|
29.0
|
1.0
|
|
CG2
|
G:VAL244
|
4.7
|
23.3
|
1.0
|
|
N
|
G:GLY125
|
4.9
|
28.7
|
1.0
|
|
CA
|
G:GLY125
|
4.9
|
28.7
|
1.0
|
|
C1
|
G:KYN302
|
5.0
|
27.0
|
1.0
|
|
CA
|
G:KYN302
|
5.0
|
26.7
|
1.0
|
|
Iron binding site 8 out
of 8 in 7p46
Go back to
Iron Binding Sites List in 7p46
Iron binding site 8 out
of 8 in the Crystal Structure of Xanthomonas Campestris Tryptophan 2,3-Dioxygenase (Tdo)
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 8 of Crystal Structure of Xanthomonas Campestris Tryptophan 2,3-Dioxygenase (Tdo) within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
H:Fe301
b:21.7
occ:1.00
|
FE
|
H:HEM301
|
0.0
|
21.7
|
1.0
|
|
ND
|
H:HEM301
|
1.9
|
20.4
|
1.0
|
|
C
|
H:CYN302
|
2.0
|
22.8
|
1.0
|
|
NA
|
H:HEM301
|
2.0
|
21.3
|
1.0
|
|
NC
|
H:HEM301
|
2.1
|
20.2
|
1.0
|
|
NB
|
H:HEM301
|
2.1
|
20.5
|
1.0
|
|
CE1
|
H:HIS240
|
2.1
|
16.9
|
1.0
|
|
NE2
|
H:HIS240
|
2.9
|
23.0
|
1.0
|
|
C1D
|
H:HEM301
|
3.0
|
21.1
|
1.0
|
|
C4D
|
H:HEM301
|
3.0
|
21.5
|
1.0
|
|
C1A
|
H:HEM301
|
3.0
|
22.9
|
1.0
|
|
C4B
|
H:HEM301
|
3.0
|
22.2
|
1.0
|
|
C4C
|
H:HEM301
|
3.1
|
21.7
|
1.0
|
|
C4A
|
H:HEM301
|
3.1
|
24.4
|
1.0
|
|
C1B
|
H:HEM301
|
3.1
|
25.1
|
1.0
|
|
C1C
|
H:HEM301
|
3.1
|
22.4
|
1.0
|
|
N
|
H:CYN302
|
3.2
|
22.6
|
1.0
|
|
ND1
|
H:HIS240
|
3.3
|
22.7
|
1.0
|
|
CHD
|
H:HEM301
|
3.4
|
21.7
|
1.0
|
|
CHA
|
H:HEM301
|
3.4
|
22.1
|
1.0
|
|
CHB
|
H:HEM301
|
3.5
|
24.1
|
1.0
|
|
CHC
|
H:HEM301
|
3.5
|
20.9
|
1.0
|
|
CD2
|
H:HIS240
|
4.1
|
18.3
|
1.0
|
|
C2A
|
H:HEM301
|
4.2
|
24.0
|
1.0
|
|
C2D
|
H:HEM301
|
4.2
|
19.9
|
1.0
|
|
C3A
|
H:HEM301
|
4.3
|
24.1
|
1.0
|
|
C3D
|
H:HEM301
|
4.3
|
21.1
|
1.0
|
|
C2B
|
H:HEM301
|
4.3
|
23.4
|
1.0
|
|
C3C
|
H:HEM301
|
4.3
|
22.1
|
1.0
|
|
C2C
|
H:HEM301
|
4.3
|
21.8
|
1.0
|
|
CG
|
H:HIS240
|
4.3
|
18.8
|
1.0
|
|
C3B
|
H:HEM301
|
4.3
|
21.7
|
1.0
|
|
O2
|
H:KYN303
|
4.3
|
24.3
|
1.0
|
|
N1
|
H:KYN303
|
4.7
|
23.7
|
1.0
|
|
CG2
|
H:VAL244
|
4.7
|
22.1
|
1.0
|
|
N
|
H:KYN303
|
4.7
|
24.1
|
1.0
|
|
N
|
H:GLY125
|
4.9
|
24.2
|
1.0
|
|
C1
|
H:KYN303
|
5.0
|
23.7
|
1.0
|
|
CA
|
H:GLY125
|
5.0
|
25.2
|
1.0
|
|
Reference:
J.Basran,
E.S.Booth,
L.P.Campbell,
S.J.Thackray,
M.H.Jesani,
J.Clayden,
P.C.E.Moody,
C.G.Mowat,
H.Kwon,
E.L.Raven.
Binding of L-Kynurenine to X. Campestris Tryptophan 2,3-Dioxygenase. J.Inorg.Biochem. V. 225 11604 2021.
ISSN: ISSN 0162-0134
PubMed: 34571402
DOI: 10.1016/J.JINORGBIO.2021.111604
Page generated: Fri Nov 5 14:06:53 2021
|
