Atomistry » Iron » PDB 7yzt-7zih » 7z2l
Atomistry »
  Iron »
    PDB 7yzt-7zih »
      7z2l »

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

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy