Iron in PDB 6e46: Crystal Structure of Human Indoleamine 2,3-Dioxygenase 1 (IDO1) in Complex with Ferrous Heme and Tryptophan
Enzymatic activity of Crystal Structure of Human Indoleamine 2,3-Dioxygenase 1 (IDO1) in Complex with Ferrous Heme and Tryptophan
All present enzymatic activity of Crystal Structure of Human Indoleamine 2,3-Dioxygenase 1 (IDO1) in Complex with Ferrous Heme and Tryptophan:
1.13.11.52;
Protein crystallography data
The structure of Crystal Structure of Human Indoleamine 2,3-Dioxygenase 1 (IDO1) in Complex with Ferrous Heme and Tryptophan, PDB code: 6e46
was solved by
S.Luo,
L.Tong,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
49.30 /
2.09
|
Space group
|
P 21 21 2
|
Cell size a, b, c (Å), α, β, γ (°)
|
79.916,
197.189,
115.016,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
20.8 /
24.7
|
Iron Binding Sites:
The binding sites of Iron atom in the Crystal Structure of Human Indoleamine 2,3-Dioxygenase 1 (IDO1) in Complex with Ferrous Heme and Tryptophan
(pdb code 6e46). This binding sites where shown within
5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the
Crystal Structure of Human Indoleamine 2,3-Dioxygenase 1 (IDO1) in Complex with Ferrous Heme and Tryptophan, PDB code: 6e46:
Jump to Iron binding site number:
1;
2;
3;
4;
Iron binding site 1 out
of 4 in 6e46
Go back to
Iron Binding Sites List in 6e46
Iron binding site 1 out
of 4 in the Crystal Structure of Human Indoleamine 2,3-Dioxygenase 1 (IDO1) in Complex with Ferrous Heme and Tryptophan
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 Human Indoleamine 2,3-Dioxygenase 1 (IDO1) in Complex with Ferrous Heme and Tryptophan within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe501
b:35.1
occ:1.00
|
FE
|
A:HEM501
|
0.0
|
35.1
|
1.0
|
NA
|
A:HEM501
|
2.1
|
32.6
|
1.0
|
NB
|
A:HEM501
|
2.1
|
33.7
|
1.0
|
NC
|
A:HEM501
|
2.1
|
36.0
|
1.0
|
ND
|
A:HEM501
|
2.1
|
33.6
|
1.0
|
NE2
|
A:HIS346
|
2.3
|
36.5
|
1.0
|
C1B
|
A:HEM501
|
3.0
|
35.3
|
1.0
|
C4A
|
A:HEM501
|
3.0
|
36.4
|
1.0
|
C4C
|
A:HEM501
|
3.0
|
38.7
|
1.0
|
C1D
|
A:HEM501
|
3.1
|
37.6
|
1.0
|
C4B
|
A:HEM501
|
3.1
|
35.8
|
1.0
|
C1A
|
A:HEM501
|
3.1
|
39.4
|
1.0
|
C1C
|
A:HEM501
|
3.1
|
35.1
|
1.0
|
C4D
|
A:HEM501
|
3.1
|
38.6
|
1.0
|
CD2
|
A:HIS346
|
3.2
|
33.5
|
1.0
|
CE1
|
A:HIS346
|
3.3
|
36.1
|
1.0
|
CHB
|
A:HEM501
|
3.3
|
34.3
|
1.0
|
CHD
|
A:HEM501
|
3.4
|
36.1
|
1.0
|
CHC
|
A:HEM501
|
3.5
|
35.2
|
1.0
|
CHA
|
A:HEM501
|
3.5
|
34.6
|
1.0
|
CD1
|
A:TRP502
|
4.0
|
42.0
|
1.0
|
NE1
|
A:TRP502
|
4.1
|
51.2
|
1.0
|
C2B
|
A:HEM501
|
4.2
|
34.6
|
1.0
|
C3C
|
A:HEM501
|
4.3
|
36.8
|
1.0
|
C3A
|
A:HEM501
|
4.3
|
38.0
|
1.0
|
C3B
|
A:HEM501
|
4.3
|
32.0
|
1.0
|
C2D
|
A:HEM501
|
4.3
|
37.7
|
1.0
|
C2A
|
A:HEM501
|
4.3
|
36.9
|
1.0
|
C2C
|
A:HEM501
|
4.3
|
37.0
|
1.0
|
C3D
|
A:HEM501
|
4.3
|
39.4
|
1.0
|
ND1
|
A:HIS346
|
4.3
|
36.2
|
1.0
|
CG
|
A:HIS346
|
4.3
|
34.8
|
1.0
|
CB
|
A:ALA264
|
4.4
|
47.1
|
1.0
|
N
|
A:ALA264
|
4.9
|
47.5
|
1.0
|
CG1
|
A:VAL350
|
5.0
|
37.9
|
1.0
|
|
Iron binding site 2 out
of 4 in 6e46
Go back to
Iron Binding Sites List in 6e46
Iron binding site 2 out
of 4 in the Crystal Structure of Human Indoleamine 2,3-Dioxygenase 1 (IDO1) in Complex with Ferrous Heme and Tryptophan
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 Human Indoleamine 2,3-Dioxygenase 1 (IDO1) in Complex with Ferrous Heme and Tryptophan within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe501
b:32.4
occ:1.00
|
FE
|
B:HEM501
|
0.0
|
32.4
|
1.0
|
NA
|
B:HEM501
|
2.0
|
32.5
|
1.0
|
NB
|
B:HEM501
|
2.0
|
32.9
|
1.0
|
NC
|
B:HEM501
|
2.1
|
35.1
|
1.0
|
ND
|
B:HEM501
|
2.1
|
33.6
|
1.0
|
NE2
|
B:HIS346
|
2.2
|
32.3
|
1.0
|
C1B
|
B:HEM501
|
3.0
|
33.5
|
1.0
|
C4A
|
B:HEM501
|
3.0
|
35.4
|
1.0
|
C4C
|
B:HEM501
|
3.1
|
37.7
|
1.0
|
C1A
|
B:HEM501
|
3.1
|
35.3
|
1.0
|
C1D
|
B:HEM501
|
3.1
|
36.4
|
1.0
|
C4D
|
B:HEM501
|
3.1
|
35.4
|
1.0
|
C4B
|
B:HEM501
|
3.1
|
35.9
|
1.0
|
C1C
|
B:HEM501
|
3.1
|
36.6
|
1.0
|
CD2
|
B:HIS346
|
3.1
|
34.3
|
1.0
|
CE1
|
B:HIS346
|
3.3
|
32.8
|
1.0
|
CHB
|
B:HEM501
|
3.3
|
32.9
|
1.0
|
CHD
|
B:HEM501
|
3.4
|
35.6
|
1.0
|
CHA
|
B:HEM501
|
3.5
|
31.9
|
1.0
|
CHC
|
B:HEM501
|
3.5
|
33.6
|
1.0
|
CD1
|
B:TRP502
|
4.0
|
39.9
|
1.0
|
NE1
|
B:TRP502
|
4.2
|
41.9
|
1.0
|
C2B
|
B:HEM501
|
4.2
|
35.2
|
1.0
|
C3A
|
B:HEM501
|
4.2
|
37.9
|
1.0
|
C3B
|
B:HEM501
|
4.3
|
35.0
|
1.0
|
CG
|
B:HIS346
|
4.3
|
34.0
|
1.0
|
C2A
|
B:HEM501
|
4.3
|
37.7
|
1.0
|
C2D
|
B:HEM501
|
4.3
|
33.4
|
1.0
|
C3C
|
B:HEM501
|
4.3
|
39.5
|
1.0
|
C2C
|
B:HEM501
|
4.3
|
39.5
|
1.0
|
C3D
|
B:HEM501
|
4.3
|
33.0
|
1.0
|
ND1
|
B:HIS346
|
4.3
|
35.3
|
1.0
|
CB
|
B:ALA264
|
4.4
|
37.2
|
1.0
|
O
|
B:HOH671
|
4.7
|
38.8
|
1.0
|
N
|
B:ALA264
|
4.9
|
39.0
|
1.0
|
|
Iron binding site 3 out
of 4 in 6e46
Go back to
Iron Binding Sites List in 6e46
Iron binding site 3 out
of 4 in the Crystal Structure of Human Indoleamine 2,3-Dioxygenase 1 (IDO1) in Complex with Ferrous Heme and Tryptophan
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 Human Indoleamine 2,3-Dioxygenase 1 (IDO1) in Complex with Ferrous Heme and Tryptophan within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Fe501
b:39.7
occ:1.00
|
FE
|
C:HEM501
|
0.0
|
39.7
|
1.0
|
NC
|
C:HEM501
|
2.0
|
43.2
|
1.0
|
NA
|
C:HEM501
|
2.0
|
38.5
|
1.0
|
ND
|
C:HEM501
|
2.1
|
42.7
|
1.0
|
NB
|
C:HEM501
|
2.1
|
40.8
|
1.0
|
NE2
|
C:HIS346
|
2.3
|
44.7
|
1.0
|
C4C
|
C:HEM501
|
3.0
|
42.2
|
1.0
|
C1D
|
C:HEM501
|
3.0
|
42.6
|
1.0
|
C4A
|
C:HEM501
|
3.0
|
43.6
|
1.0
|
C1B
|
C:HEM501
|
3.1
|
42.6
|
1.0
|
C1C
|
C:HEM501
|
3.1
|
43.0
|
1.0
|
C1A
|
C:HEM501
|
3.1
|
46.1
|
1.0
|
C4D
|
C:HEM501
|
3.1
|
41.3
|
1.0
|
C4B
|
C:HEM501
|
3.1
|
41.6
|
1.0
|
CD2
|
C:HIS346
|
3.2
|
45.0
|
1.0
|
CE1
|
C:HIS346
|
3.3
|
43.8
|
1.0
|
CHD
|
C:HEM501
|
3.4
|
41.7
|
1.0
|
CHB
|
C:HEM501
|
3.4
|
42.5
|
1.0
|
CHC
|
C:HEM501
|
3.5
|
42.8
|
1.0
|
CHA
|
C:HEM501
|
3.5
|
45.0
|
1.0
|
CD1
|
C:TRP503
|
4.0
|
47.2
|
1.0
|
NE1
|
C:TRP503
|
4.1
|
51.1
|
1.0
|
CB
|
C:ALA264
|
4.1
|
51.0
|
1.0
|
C3C
|
C:HEM501
|
4.2
|
43.9
|
1.0
|
C2C
|
C:HEM501
|
4.2
|
41.8
|
1.0
|
C2D
|
C:HEM501
|
4.3
|
44.3
|
1.0
|
C3A
|
C:HEM501
|
4.3
|
45.3
|
1.0
|
C2B
|
C:HEM501
|
4.3
|
40.6
|
1.0
|
C2A
|
C:HEM501
|
4.3
|
46.1
|
1.0
|
C3D
|
C:HEM501
|
4.3
|
43.0
|
1.0
|
CG
|
C:HIS346
|
4.3
|
45.3
|
1.0
|
C3B
|
C:HEM501
|
4.3
|
39.6
|
1.0
|
ND1
|
C:HIS346
|
4.4
|
44.6
|
1.0
|
N
|
C:ALA264
|
4.8
|
54.6
|
1.0
|
CA
|
C:ALA264
|
5.0
|
43.8
|
1.0
|
|
Iron binding site 4 out
of 4 in 6e46
Go back to
Iron Binding Sites List in 6e46
Iron binding site 4 out
of 4 in the Crystal Structure of Human Indoleamine 2,3-Dioxygenase 1 (IDO1) in Complex with Ferrous Heme and Tryptophan
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 Human Indoleamine 2,3-Dioxygenase 1 (IDO1) in Complex with Ferrous Heme and Tryptophan within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Fe501
b:38.9
occ:1.00
|
FE
|
D:HEM501
|
0.0
|
38.9
|
1.0
|
NB
|
D:HEM501
|
2.0
|
37.4
|
1.0
|
NA
|
D:HEM501
|
2.0
|
38.1
|
1.0
|
ND
|
D:HEM501
|
2.0
|
37.1
|
1.0
|
NC
|
D:HEM501
|
2.1
|
38.0
|
1.0
|
NE2
|
D:HIS346
|
2.3
|
37.4
|
1.0
|
C1B
|
D:HEM501
|
3.0
|
37.2
|
1.0
|
C4A
|
D:HEM501
|
3.0
|
39.4
|
1.0
|
C1D
|
D:HEM501
|
3.0
|
42.4
|
1.0
|
C4C
|
D:HEM501
|
3.0
|
38.0
|
1.0
|
C4B
|
D:HEM501
|
3.1
|
39.9
|
1.0
|
C4D
|
D:HEM501
|
3.1
|
39.0
|
1.0
|
C1A
|
D:HEM501
|
3.1
|
40.5
|
1.0
|
C1C
|
D:HEM501
|
3.1
|
34.0
|
1.0
|
CD2
|
D:HIS346
|
3.2
|
40.3
|
1.0
|
CE1
|
D:HIS346
|
3.3
|
39.3
|
1.0
|
CHB
|
D:HEM501
|
3.3
|
35.7
|
1.0
|
CHD
|
D:HEM501
|
3.3
|
38.1
|
1.0
|
CHA
|
D:HEM501
|
3.5
|
37.7
|
1.0
|
CHC
|
D:HEM501
|
3.5
|
36.7
|
1.0
|
CD1
|
D:TRP503
|
3.8
|
41.6
|
1.0
|
NE1
|
D:TRP503
|
4.0
|
47.0
|
1.0
|
C2B
|
D:HEM501
|
4.2
|
36.4
|
1.0
|
C3A
|
D:HEM501
|
4.2
|
42.8
|
1.0
|
C2D
|
D:HEM501
|
4.3
|
42.5
|
1.0
|
C3B
|
D:HEM501
|
4.3
|
35.1
|
1.0
|
C3C
|
D:HEM501
|
4.3
|
39.9
|
1.0
|
C3D
|
D:HEM501
|
4.3
|
38.6
|
1.0
|
C2A
|
D:HEM501
|
4.3
|
43.4
|
1.0
|
CG
|
D:HIS346
|
4.3
|
36.3
|
1.0
|
C2C
|
D:HEM501
|
4.3
|
37.0
|
1.0
|
ND1
|
D:HIS346
|
4.3
|
39.8
|
1.0
|
CB
|
D:ALA264
|
4.4
|
47.8
|
1.0
|
N
|
D:ALA264
|
4.8
|
46.0
|
1.0
|
O
|
D:HOH623
|
4.8
|
45.2
|
1.0
|
|
Reference:
S.Luo,
K.Xu,
S.Xiang,
J.Chen,
C.Chen,
C.Guo,
Y.Tong,
L.Tong.
High-Resolution Structures of Inhibitor Complexes of Human Indoleamine 2,3-Dioxygenase 1 in A New Crystal Form. Acta Crystallogr F Struct V. 74 717 2018BIOL Commun.
ISSN: ESSN 2053-230X
PubMed: 30387777
DOI: 10.1107/S2053230X18012955
Page generated: Tue Aug 6 17:18:15 2024
|