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Iron in PDB 7yxt: Crystal Structure of Human Indoleamine-2,3-Dioxygenase 1 (HIDO1) with Different Conformations For G261-G265 Fragment

Enzymatic activity of Crystal Structure of Human Indoleamine-2,3-Dioxygenase 1 (HIDO1) with Different Conformations For G261-G265 Fragment

All present enzymatic activity of Crystal Structure of Human Indoleamine-2,3-Dioxygenase 1 (HIDO1) with Different Conformations For G261-G265 Fragment:
1.13.11.52;

Protein crystallography data

The structure of Crystal Structure of Human Indoleamine-2,3-Dioxygenase 1 (HIDO1) with Different Conformations For G261-G265 Fragment, PDB code: 7yxt 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) 49.07 / 2.48
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 81.04, 117.61, 217.18, 90, 90, 90
R / Rfree (%) 19.6 / 25.9

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of Human Indoleamine-2,3-Dioxygenase 1 (HIDO1) with Different Conformations For G261-G265 Fragment (pdb code 7yxt). 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 (HIDO1) with Different Conformations For G261-G265 Fragment, PDB code: 7yxt:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 7yxt

Go back to Iron Binding Sites List in 7yxt
Iron binding site 1 out of 4 in the Crystal Structure of Human Indoleamine-2,3-Dioxygenase 1 (HIDO1) with Different Conformations For G261-G265 Fragment


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 (HIDO1) with Different Conformations For G261-G265 Fragment within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe501

b:63.2
occ:1.00
FE A:HEM501 0.0 63.2 1.0
NC A:HEM501 2.0 60.1 1.0
ND A:HEM501 2.0 62.5 1.0
NA A:HEM501 2.1 59.7 1.0
NB A:HEM501 2.2 57.3 1.0
NE2 A:HIS346 2.3 58.6 1.0
C4C A:HEM501 2.9 60.4 1.0
C1D A:HEM501 2.9 62.8 1.0
C4D A:HEM501 3.0 65.6 1.0
C1C A:HEM501 3.1 51.8 1.0
C4A A:HEM501 3.1 58.4 1.0
C1A A:HEM501 3.1 62.3 1.0
CE1 A:HIS346 3.1 57.9 1.0
C1B A:HEM501 3.1 55.8 1.0
C4B A:HEM501 3.2 49.2 1.0
CD2 A:HIS346 3.2 61.1 1.0
CHD A:HEM501 3.2 58.9 1.0
CB A:ALA264 3.4 58.5 1.0
CHA A:HEM501 3.5 63.1 1.0
CHB A:HEM501 3.5 56.0 1.0
CHC A:HEM501 3.5 49.4 1.0
C A:ALA264 3.9 65.6 1.0
N A:GLY265 4.1 61.8 1.0
C3C A:HEM501 4.1 55.2 1.0
O A:ALA264 4.2 62.3 1.0
C2D A:HEM501 4.2 67.2 1.0
C2C A:HEM501 4.2 53.6 1.0
ND1 A:HIS346 4.2 59.5 1.0
C3D A:HEM501 4.2 72.0 1.0
CA A:ALA264 4.2 63.5 1.0
CG A:HIS346 4.3 56.6 1.0
C3A A:HEM501 4.3 61.4 1.0
C2A A:HEM501 4.3 60.5 1.0
C2B A:HEM501 4.4 54.0 1.0
C3B A:HEM501 4.4 51.9 1.0
CA A:GLY265 4.4 57.8 1.0

Iron binding site 2 out of 4 in 7yxt

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Iron binding site 2 out of 4 in the Crystal Structure of Human Indoleamine-2,3-Dioxygenase 1 (HIDO1) with Different Conformations For G261-G265 Fragment


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 (HIDO1) with Different Conformations For G261-G265 Fragment within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe501

b:61.0
occ:1.00
FE B:HEM501 0.0 61.0 1.0
NE2 B:HIS346 2.0 58.8 1.0
NC B:HEM501 2.0 62.1 1.0
ND B:HEM501 2.0 66.0 1.0
NA B:HEM501 2.1 56.3 1.0
NB B:HEM501 2.2 59.5 1.0
O B:ALA264 2.3 57.6 0.8
CD2 B:HIS346 2.9 60.2 1.0
C4C B:HEM501 3.0 58.5 1.0
C1C B:HEM501 3.0 53.5 1.0
C1D B:HEM501 3.1 64.3 1.0
C4D B:HEM501 3.1 67.4 1.0
CE1 B:HIS346 3.1 63.9 1.0
C1A B:HEM501 3.1 60.6 1.0
C4B B:HEM501 3.1 55.0 1.0
C4A B:HEM501 3.2 56.7 1.0
C1B B:HEM501 3.2 60.2 1.0
CHD B:HEM501 3.4 56.3 1.0
CHA B:HEM501 3.4 64.5 1.0
CHC B:HEM501 3.4 52.1 1.0
C B:ALA264 3.6 59.2 0.8
CHB B:HEM501 3.6 58.3 1.0
CB B:ALA264 3.6 57.2 0.2
C B:ALA264 4.0 57.2 0.2
CG B:HIS346 4.1 62.0 1.0
CB B:ALA264 4.1 55.2 0.8
O B:ALA264 4.1 55.2 0.2
ND1 B:HIS346 4.1 65.5 1.0
C3C B:HEM501 4.2 57.5 1.0
C2C B:HEM501 4.2 54.9 1.0
C2D B:HEM501 4.3 69.0 1.0
C3D B:HEM501 4.3 70.5 1.0
N B:GLY265 4.3 57.0 0.2
C2A B:HEM501 4.4 61.9 1.0
CA B:ALA264 4.4 57.0 0.2
C3B B:HEM501 4.4 58.1 1.0
CA B:ALA264 4.4 57.1 0.8
C3A B:HEM501 4.4 58.0 1.0
C2B B:HEM501 4.4 58.8 1.0
CA B:GLY265 4.5 56.5 0.2
N B:GLY265 4.5 57.0 0.8
CA B:GLY265 4.6 56.4 0.8
O B:HOH684 4.8 52.3 1.0
CG2 B:VAL350 5.0 58.9 1.0

Iron binding site 3 out of 4 in 7yxt

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Iron binding site 3 out of 4 in the Crystal Structure of Human Indoleamine-2,3-Dioxygenase 1 (HIDO1) with Different Conformations For G261-G265 Fragment


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 (HIDO1) with Different Conformations For G261-G265 Fragment within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Fe501

b:58.4
occ:1.00
FE C:HEM501 0.0 58.4 1.0
NC C:HEM501 2.0 55.8 1.0
ND C:HEM501 2.1 60.8 1.0
NB C:HEM501 2.1 52.6 1.0
NA C:HEM501 2.1 55.0 1.0
NE2 C:HIS346 2.3 53.2 1.0
C4C C:HEM501 3.0 52.5 1.0
C1D C:HEM501 3.0 59.1 1.0
C1C C:HEM501 3.0 50.6 1.0
C4B C:HEM501 3.1 53.5 1.0
C4D C:HEM501 3.1 61.6 1.0
C4A C:HEM501 3.1 51.5 1.0
C1B C:HEM501 3.2 51.6 1.0
C1A C:HEM501 3.2 51.3 1.0
CE1 C:HIS346 3.2 46.2 1.0
CHD C:HEM501 3.4 53.9 1.0
CD2 C:HIS346 3.4 50.8 1.0
CHC C:HEM501 3.4 51.6 1.0
CB C:ALA264 3.5 62.2 1.0
CHB C:HEM501 3.5 52.4 1.0
CHA C:HEM501 3.5 54.1 1.0
C C:ALA264 4.1 69.2 1.0
N C:GLY265 4.1 60.3 1.0
C3C C:HEM501 4.2 47.5 1.0
C2C C:HEM501 4.2 54.2 1.0
C2D C:HEM501 4.3 59.9 1.0
CA C:ALA264 4.3 68.6 1.0
C3D C:HEM501 4.3 61.9 1.0
C3B C:HEM501 4.3 49.0 1.0
ND1 C:HIS346 4.4 51.6 1.0
C2B C:HEM501 4.4 50.8 1.0
C3A C:HEM501 4.4 53.9 1.0
C2A C:HEM501 4.4 52.1 1.0
O C:ALA264 4.4 65.5 1.0
CG C:HIS346 4.5 48.0 1.0
CA C:GLY265 4.5 51.1 1.0
N C:ALA264 4.8 67.6 1.0

Iron binding site 4 out of 4 in 7yxt

Go back to Iron Binding Sites List in 7yxt
Iron binding site 4 out of 4 in the Crystal Structure of Human Indoleamine-2,3-Dioxygenase 1 (HIDO1) with Different Conformations For G261-G265 Fragment


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 (HIDO1) with Different Conformations For G261-G265 Fragment within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe501

b:52.9
occ:1.00
FE D:HEM501 0.0 52.9 1.0
ND D:HEM501 2.0 52.5 1.0
NC D:HEM501 2.0 52.2 1.0
NE2 D:HIS346 2.1 52.6 1.0
NB D:HEM501 2.1 47.0 1.0
NA D:HEM501 2.1 49.7 1.0
O D:ALA264 2.3 55.4 0.5
C1D D:HEM501 3.0 57.0 1.0
CE1 D:HIS346 3.0 46.1 1.0
C4C D:HEM501 3.0 53.6 1.0
C4D D:HEM501 3.0 54.8 1.0
C1C D:HEM501 3.1 47.1 1.0
CD2 D:HIS346 3.1 48.1 1.0
C4B D:HEM501 3.1 52.0 1.0
C1B D:HEM501 3.1 51.5 1.0
C1A D:HEM501 3.1 51.7 1.0
C4A D:HEM501 3.2 50.0 1.0
CHD D:HEM501 3.3 56.4 1.0
CHC D:HEM501 3.4 50.2 1.0
C D:ALA264 3.4 55.0 0.5
CHA D:HEM501 3.5 51.5 1.0
CHB D:HEM501 3.5 53.4 1.0
CB D:ALA264 3.6 51.4 0.5
CB D:ALA264 4.0 54.2 0.5
ND1 D:HIS346 4.1 45.4 1.0
N D:GLY265 4.2 53.7 0.5
CG D:HIS346 4.2 46.1 1.0
C2D D:HEM501 4.2 59.5 1.0
C D:ALA264 4.2 54.5 0.5
CA D:ALA264 4.2 54.9 0.5
C3C D:HEM501 4.2 50.4 1.0
C3D D:HEM501 4.2 59.4 1.0
C2C D:HEM501 4.3 50.3 1.0
C3B D:HEM501 4.3 51.6 1.0
C2B D:HEM501 4.3 53.3 1.0
C2A D:HEM501 4.4 52.1 1.0
C3A D:HEM501 4.4 52.6 1.0
N D:GLY265 4.4 54.5 0.5
CA D:ALA264 4.5 53.1 0.5
CA D:GLY265 4.6 52.1 0.5
O D:HOH699 4.6 59.1 0.9
O D:ALA264 4.6 52.0 0.5
CA D:GLY265 4.9 52.5 0.5

Reference:

M.Mirgaux, J.Wouters. Crystal Structure of Human Indoleamine-2,3-Dioxygenase 1 (HIDO1) with Different Conformations For G261-G265 Fragment To Be Published.
Page generated: Fri Aug 9 12:29:24 2024

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