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Iron in PDB 7z2l: Crystal Structure of L-Kynurenine in the Active Site of Human Indoleamine-2,3-Dioxygenase 1 (HIDO1)

Enzymatic activity of Crystal Structure of L-Kynurenine in the Active Site of Human Indoleamine-2,3-Dioxygenase 1 (HIDO1)

All present enzymatic activity of Crystal Structure of L-Kynurenine in the Active Site of Human Indoleamine-2,3-Dioxygenase 1 (HIDO1):
1.13.11.52;

Protein crystallography data

The structure of Crystal Structure of L-Kynurenine in the Active Site of Human Indoleamine-2,3-Dioxygenase 1 (HIDO1), PDB code: 7z2l was solved by M.Mirgaux, J.Wouters, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 47.23 / 2.56
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 81, 116.28, 217.59, 90, 90, 90
R / Rfree (%) 18 / 24.4

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of L-Kynurenine in the Active Site of Human Indoleamine-2,3-Dioxygenase 1 (HIDO1) (pdb code 7z2l). 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 L-Kynurenine in the Active Site of Human Indoleamine-2,3-Dioxygenase 1 (HIDO1), PDB code: 7z2l:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 7z2l

Go back to Iron Binding Sites List in 7z2l
Iron binding site 1 out of 4 in the Crystal Structure of L-Kynurenine in the Active Site of Human Indoleamine-2,3-Dioxygenase 1 (HIDO1)


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 L-Kynurenine in the Active Site of Human Indoleamine-2,3-Dioxygenase 1 (HIDO1) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe501

b:54.9
occ:1.00
 FE A:HEM501 0.0 54.9 1.0
ND A:HEM501 1.9 55.8 1.0
NC A:HEM501 2.0 47.8 1.0
NA A:HEM501 2.1 53.9 1.0
NB A:HEM501 2.1 48.5 1.0
NE2 A:HIS346 2.2 48.4 1.0
C4D A:HEM501 3.0 57.3 1.0
C1D A:HEM501 3.0 55.5 1.0
CD2 A:HIS346 3.0 50.2 1.0
C4C A:HEM501 3.0 45.6 1.0
C1C A:HEM501 3.1 42.1 1.0
C1A A:HEM501 3.1 52.0 1.0
C4B A:HEM501 3.1 40.9 1.0
C4A A:HEM501 3.2 52.2 1.0
C1B A:HEM501 3.2 48.2 1.0
CE1 A:HIS346 3.3 53.8 1.0
CHD A:HEM501 3.4 50.7 1.0
CB A:ALA264 3.4 47.4 1.0
CHA A:HEM501 3.4 51.7 1.0
CHC A:HEM501 3.4 40.1 1.0
CHB A:HEM501 3.5 51.0 1.0
C A:ALA264 4.0 58.0 1.0
O A:ALA264 4.0 54.8 1.0
C3D A:HEM501 4.1 66.3 1.0
C2D A:HEM501 4.1 62.3 1.0
CG A:HIS346 4.2 52.1 1.0
CA A:ALA264 4.2 53.8 1.0
C3C A:HEM501 4.3 47.4 1.0
C2C A:HEM501 4.3 45.9 1.0
ND1 A:HIS346 4.3 55.2 1.0
N A:GLY265 4.4 56.9 1.0
C2A A:HEM501 4.4 52.0 1.0
C3B A:HEM501 4.4 46.4 1.0
C3A A:HEM501 4.4 49.0 1.0
C2B A:HEM501 4.4 45.3 1.0
CA A:GLY265 4.8 49.8 1.0

Iron binding site 2 out of 4 in 7z2l

Go back to Iron Binding Sites List in 7z2l
Iron binding site 2 out of 4 in the Crystal Structure of L-Kynurenine in the Active Site of Human Indoleamine-2,3-Dioxygenase 1 (HIDO1)


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 L-Kynurenine in the Active Site of Human Indoleamine-2,3-Dioxygenase 1 (HIDO1) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe501

b:51.5
occ:1.00
 FE B:HEM501 0.0 51.5 1.0
ND B:HEM501 2.0 57.7 1.0
NC B:HEM501 2.0 52.8 1.0
NA B:HEM501 2.1 51.8 1.0
NB B:HEM501 2.2 49.6 1.0
NE2 B:HIS346 2.2 49.7 1.0
O1 B:OXY506 2.4 55.4 0.4
O B:ALA264 2.6 51.1 0.6
CD2 B:HIS346 2.9 53.6 1.0
C4D B:HEM501 3.0 59.7 1.0
C1D B:HEM501 3.0 58.0 1.0
C1C B:HEM501 3.0 48.5 1.0
C4C B:HEM501 3.0 51.3 1.0
C1A B:HEM501 3.1 52.9 1.0
C4B B:HEM501 3.1 45.0 1.0
C4A B:HEM501 3.2 51.4 1.0
C1B B:HEM501 3.2 49.7 1.0
CE1 B:HIS346 3.3 54.1 1.0
CHD B:HEM501 3.4 54.6 1.0
CHA B:HEM501 3.4 56.4 1.0
CHC B:HEM501 3.4 45.4 1.0
O2 B:OXY506 3.5 54.6 0.4
CHB B:HEM501 3.6 50.0 1.0
C B:ALA264 3.8 52.2 0.6
CB B:ALA264 4.0 52.7 0.6
CG B:HIS346 4.2 53.8 1.0
C3D B:HEM501 4.2 65.1 1.0
C2D B:HEM501 4.2 59.9 1.0
C3C B:HEM501 4.2 51.7 1.0
C2C B:HEM501 4.2 50.1 1.0
O B:ALA264 4.3 47.1 0.4
ND1 B:HIS346 4.3 56.2 1.0
C2A B:HEM501 4.4 55.6 1.0
C3B B:HEM501 4.4 49.1 1.0
C3A B:HEM501 4.4 52.2 1.0
C2B B:HEM501 4.4 47.7 1.0
CA B:ALA264 4.5 50.9 0.6
C B:ALA264 4.5 50.7 0.4
N B:GLY265 4.5 52.6 0.4
N B:GLY265 4.7 52.6 0.6
CB B:ALA264 4.8 50.8 0.4
CA B:GLY265 4.8 52.2 0.4
CA B:GLY265 4.8 52.1 0.6
CG2 B:VAL350 5.0 52.7 1.0

Iron binding site 3 out of 4 in 7z2l

Go back to Iron Binding Sites List in 7z2l
Iron binding site 3 out of 4 in the Crystal Structure of L-Kynurenine in the Active Site of Human Indoleamine-2,3-Dioxygenase 1 (HIDO1)


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 L-Kynurenine in the Active Site of Human Indoleamine-2,3-Dioxygenase 1 (HIDO1) within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Fe501

b:48.8
occ:1.00
 FE C:HEM501 0.0 48.8 1.0
ND C:HEM501 2.0 47.0 1.0
NB C:HEM501 2.1 42.6 1.0
NA C:HEM501 2.1 44.2 1.0
NC C:HEM501 2.1 49.2 1.0
O C:ALA264 2.2 58.9 1.0
NE2 C:HIS346 2.3 45.7 1.0
C1D C:HEM501 3.0 48.9 1.0
C4D C:HEM501 3.0 50.0 1.0
C1B C:HEM501 3.1 42.4 1.0
C4C C:HEM501 3.1 46.4 1.0
C4A C:HEM501 3.1 43.5 1.0
C1A C:HEM501 3.1 45.8 1.0
C4B C:HEM501 3.1 46.5 1.0
C1C C:HEM501 3.2 44.0 1.0
CD2 C:HIS346 3.2 40.2 1.0
CE1 C:HIS346 3.4 42.6 1.0
CHD C:HEM501 3.4 47.5 1.0
C C:ALA264 3.4 57.8 1.0
CHA C:HEM501 3.4 47.1 1.0
CHB C:HEM501 3.4 42.6 1.0
CHC C:HEM501 3.5 43.8 1.0
CB C:ALA264 3.9 49.1 1.0
CA C:ALA264 4.2 53.9 1.0
C2D C:HEM501 4.2 48.0 1.0
C3D C:HEM501 4.2 53.1 1.0
C2B C:HEM501 4.3 46.0 1.0
C3B C:HEM501 4.3 43.5 1.0
C3C C:HEM501 4.3 41.9 1.0
C3A C:HEM501 4.3 44.7 1.0
C2A C:HEM501 4.3 45.2 1.0
N C:GLY265 4.3 45.7 1.0
CG C:HIS346 4.4 41.1 1.0
C2C C:HEM501 4.4 46.1 1.0
ND1 C:HIS346 4.4 42.9 1.0
CA C:GLY265 4.4 42.7 1.0
O C:HOH677 4.7 43.2 1.0

Iron binding site 4 out of 4 in 7z2l

Go back to Iron Binding Sites List in 7z2l
Iron binding site 4 out of 4 in the Crystal Structure of L-Kynurenine in the Active Site of Human Indoleamine-2,3-Dioxygenase 1 (HIDO1)


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 L-Kynurenine in the Active Site of Human Indoleamine-2,3-Dioxygenase 1 (HIDO1) within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe501

b:50.9
occ:1.00
 FE D:HEM501 0.0 50.9 1.0
ND D:HEM501 2.0 50.8 1.0
NC D:HEM501 2.1 44.7 1.0
NB D:HEM501 2.1 44.5 1.0
NA D:HEM501 2.1 44.3 1.0
NE2 D:HIS346 2.2 43.7 1.0
C1D D:HEM501 3.0 48.7 1.0
C4C D:HEM501 3.0 41.0 1.0
CE1 D:HIS346 3.1 42.8 1.0
C4D D:HEM501 3.1 53.9 1.0
C4B D:HEM501 3.1 46.0 1.0
C1B D:HEM501 3.1 41.6 1.0
C1C D:HEM501 3.1 37.8 1.0
C4A D:HEM501 3.1 42.2 1.0
C1A D:HEM501 3.2 43.9 1.0
CD2 D:HIS346 3.2 39.3 1.0
CHD D:HEM501 3.3 45.1 1.0
CB D:ALA264 3.5 50.0 1.0
CHB D:HEM501 3.5 41.9 1.0
CHC D:HEM501 3.5 38.7 1.0
CHA D:HEM501 3.5 46.0 1.0
O D:ALA264 3.7 59.6 1.0
C D:ALA264 3.9 57.0 1.0
O D:HOH622 4.0 51.4 1.0
C2D D:HEM501 4.2 50.3 1.0
ND1 D:HIS346 4.2 39.5 1.0
C3C D:HEM501 4.3 40.5 1.0
C3D D:HEM501 4.3 55.2 1.0
CA D:ALA264 4.3 57.1 1.0
C3B D:HEM501 4.3 41.7 1.0
CG D:HIS346 4.3 38.1 1.0
C2C D:HEM501 4.3 45.2 1.0
C2B D:HEM501 4.3 41.4 1.0
C3A D:HEM501 4.4 42.6 1.0
C2A D:HEM501 4.4 47.0 1.0
N D:GLY265 4.4 48.4 1.0
CA D:GLY265 5.0 46.8 1.0
N D:ALA264 5.0 55.0 1.0

Reference:

M.Mirgaux, J.Wouters. Crystal Structure of L-Kynurenine in the Active Site of Human Indoleamine-2,3-Dioxygenase 1 (HIDO1) To Be Published.
Page generated: Fri Aug 9 13:00:57 2024

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