Atomistry » Iron » PDB 6e45-6f0a » 6e45
Atomistry »
  Iron »
    PDB 6e45-6f0a »
      6e45 »

Iron in PDB 6e45: Crystal Structure of Human Indoleamine 2,3-Dioxygenase 1 (IDO1) Free Enzyme in the Ferrous State

Enzymatic activity of Crystal Structure of Human Indoleamine 2,3-Dioxygenase 1 (IDO1) Free Enzyme in the Ferrous State

All present enzymatic activity of Crystal Structure of Human Indoleamine 2,3-Dioxygenase 1 (IDO1) Free Enzyme in the Ferrous State:
1.13.11.52;

Protein crystallography data

The structure of Crystal Structure of Human Indoleamine 2,3-Dioxygenase 1 (IDO1) Free Enzyme in the Ferrous State, PDB code: 6e45 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) 65.88 / 2.00
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 79.969, 196.538, 116.207, 90.00, 90.00, 90.00
R / Rfree (%) 18.9 / 22.6

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of Human Indoleamine 2,3-Dioxygenase 1 (IDO1) Free Enzyme in the Ferrous State (pdb code 6e45). 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) Free Enzyme in the Ferrous State, PDB code: 6e45:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 6e45

Go back to Iron Binding Sites List in 6e45
Iron binding site 1 out of 4 in the Crystal Structure of Human Indoleamine 2,3-Dioxygenase 1 (IDO1) Free Enzyme in the Ferrous State


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) Free Enzyme in the Ferrous State within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe501

b:33.1
occ:1.00
 FE A:HEM501 0.0 33.1 1.0
NA A:HEM501 2.0 30.7 1.0
NC A:HEM501 2.0 29.9 1.0
NB A:HEM501 2.1 28.6 1.0
ND A:HEM501 2.1 30.3 1.0
NE2 A:HIS346 2.2 35.0 1.0
C4A A:HEM501 3.0 32.3 1.0
C1B A:HEM501 3.0 29.3 1.0
C4C A:HEM501 3.0 31.1 1.0
C1A A:HEM501 3.1 34.1 1.0
C1D A:HEM501 3.1 29.6 1.0
C1C A:HEM501 3.1 29.8 1.0
C4B A:HEM501 3.1 28.3 1.0
CD2 A:HIS346 3.1 34.5 1.0
C4D A:HEM501 3.1 30.8 1.0
CE1 A:HIS346 3.2 37.7 1.0
CHB A:HEM501 3.4 29.4 1.0
CHD A:HEM501 3.4 31.1 1.0
CHA A:HEM501 3.5 31.9 1.0
CHC A:HEM501 3.5 29.4 1.0
CB A:ALA264 4.0 31.6 1.0
C3A A:HEM501 4.2 35.7 1.0
C2B A:HEM501 4.2 30.5 1.0
ND1 A:HIS346 4.3 33.4 1.0
C3C A:HEM501 4.3 29.1 1.0
C2A A:HEM501 4.3 33.4 1.0
O A:HOH756 4.3 36.5 1.0
CG A:HIS346 4.3 35.0 1.0
C3B A:HEM501 4.3 28.8 1.0
C2C A:HEM501 4.3 31.7 1.0
C2D A:HEM501 4.3 36.2 1.0
C3D A:HEM501 4.3 32.1 1.0
N A:GLY265 4.5 29.8 1.0
C A:ALA264 4.6 30.5 1.0
CA A:ALA264 4.8 32.1 1.0

Iron binding site 2 out of 4 in 6e45

Go back to Iron Binding Sites List in 6e45
Iron binding site 2 out of 4 in the Crystal Structure of Human Indoleamine 2,3-Dioxygenase 1 (IDO1) Free Enzyme in the Ferrous State


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) Free Enzyme in the Ferrous State within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe501

b:30.7
occ:1.00
 FE B:HEM501 0.0 30.7 1.0
NA B:HEM501 2.0 32.2 1.0
NB B:HEM501 2.0 28.3 1.0
NC B:HEM501 2.0 32.4 1.0
ND B:HEM501 2.1 31.0 1.0
NE2 B:HIS346 2.2 30.8 1.0
C1B B:HEM501 3.0 29.4 1.0
C4A B:HEM501 3.0 34.4 1.0
C4C B:HEM501 3.0 33.4 1.0
C4B B:HEM501 3.1 31.1 1.0
C1A B:HEM501 3.1 33.7 1.0
C1C B:HEM501 3.1 27.9 1.0
C1D B:HEM501 3.1 32.6 1.0
C4D B:HEM501 3.1 30.5 1.0
CD2 B:HIS346 3.1 30.8 1.0
CE1 B:HIS346 3.2 31.1 1.0
CHB B:HEM501 3.3 28.7 1.0
CHD B:HEM501 3.4 32.1 1.0
CHC B:HEM501 3.5 29.9 1.0
CHA B:HEM501 3.5 31.6 1.0
CB B:ALA264 3.9 29.9 1.0
C2B B:HEM501 4.2 29.5 1.0
C3A B:HEM501 4.2 34.8 1.0
C3B B:HEM501 4.2 29.4 1.0
C3C B:HEM501 4.3 29.3 1.0
ND1 B:HIS346 4.3 30.1 1.0
C2A B:HEM501 4.3 36.2 1.0
C2C B:HEM501 4.3 32.8 1.0
CG B:HIS346 4.3 29.2 1.0
C2D B:HEM501 4.3 34.2 1.0
O B:HOH800 4.3 35.1 1.0
C3D B:HEM501 4.3 30.2 1.0
N B:GLY265 4.6 28.4 1.0
C B:ALA264 4.6 29.4 1.0
CA B:ALA264 4.8 28.5 1.0

Iron binding site 3 out of 4 in 6e45

Go back to Iron Binding Sites List in 6e45
Iron binding site 3 out of 4 in the Crystal Structure of Human Indoleamine 2,3-Dioxygenase 1 (IDO1) Free Enzyme in the Ferrous State


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) Free Enzyme in the Ferrous State within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Fe501

b:28.9
occ:1.00
 FE C:HEM501 0.0 28.9 1.0
NC C:HEM501 2.0 25.5 1.0
NB C:HEM501 2.0 28.7 1.0
NA C:HEM501 2.1 29.6 1.0
NE2 C:HIS346 2.1 29.7 1.0
ND C:HEM501 2.1 29.2 1.0
C1B C:HEM501 3.0 28.0 1.0
CE1 C:HIS346 3.0 29.8 1.0
C4C C:HEM501 3.0 26.2 1.0
C4A C:HEM501 3.0 30.9 1.0
CD2 C:HIS346 3.1 26.5 1.0
C1C C:HEM501 3.1 26.2 1.0
C4B C:HEM501 3.1 27.1 1.0
C1D C:HEM501 3.1 28.8 1.0
C1A C:HEM501 3.1 33.1 1.0
C4D C:HEM501 3.1 29.1 1.0
CHB C:HEM501 3.4 30.7 1.0
CHD C:HEM501 3.4 28.3 1.0
CHC C:HEM501 3.5 25.1 1.0
CHA C:HEM501 3.5 31.0 1.0
CB C:ALA264 4.0 28.0 1.0
ND1 C:HIS346 4.1 28.3 1.0
CG C:HIS346 4.2 29.9 1.0
O C:HOH787 4.2 31.3 1.0
C2B C:HEM501 4.2 29.8 1.0
C3C C:HEM501 4.2 27.2 1.0
C3B C:HEM501 4.3 28.1 1.0
C2C C:HEM501 4.3 25.2 1.0
C3A C:HEM501 4.3 36.2 1.0
C2A C:HEM501 4.3 34.2 1.0
C2D C:HEM501 4.3 31.8 1.0
C3D C:HEM501 4.3 29.5 1.0
N C:GLY265 4.5 27.5 1.0
C C:ALA264 4.6 28.2 1.0
CA C:ALA264 4.8 29.4 1.0
CG2 C:VAL350 4.9 28.7 1.0

Iron binding site 4 out of 4 in 6e45

Go back to Iron Binding Sites List in 6e45
Iron binding site 4 out of 4 in the Crystal Structure of Human Indoleamine 2,3-Dioxygenase 1 (IDO1) Free Enzyme in the Ferrous State


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) Free Enzyme in the Ferrous State within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe501

b:27.4
occ:1.00
 FE D:HEM501 0.0 27.4 1.0
NB D:HEM501 2.0 26.5 1.0
NA D:HEM501 2.0 29.4 1.0
ND D:HEM501 2.0 29.6 1.0
NC D:HEM501 2.1 27.6 1.0
NE2 D:HIS346 2.2 25.6 1.0
C1B D:HEM501 3.0 25.7 1.0
C4A D:HEM501 3.0 30.7 1.0
C1D D:HEM501 3.1 27.0 1.0
CE1 D:HIS346 3.1 28.0 1.0
C4B D:HEM501 3.1 27.6 1.0
C4D D:HEM501 3.1 29.2 1.0
C4C D:HEM501 3.1 28.8 1.0
C1A D:HEM501 3.1 30.1 1.0
C1C D:HEM501 3.1 25.0 1.0
CD2 D:HIS346 3.2 28.9 1.0
CHB D:HEM501 3.4 26.8 1.0
CHD D:HEM501 3.4 28.6 1.0
CHA D:HEM501 3.4 30.8 1.0
CHC D:HEM501 3.5 25.5 1.0
O D:HOH765 4.0 33.0 1.0
CB D:ALA264 4.0 28.4 1.0
ND1 D:HIS346 4.2 25.4 1.0
C2B D:HEM501 4.2 26.9 1.0
C3B D:HEM501 4.3 26.0 1.0
CG D:HIS346 4.3 28.0 1.0
C3A D:HEM501 4.3 32.4 1.0
C2D D:HEM501 4.3 27.9 1.0
C3D D:HEM501 4.3 28.1 1.0
C2A D:HEM501 4.3 32.6 1.0
C3C D:HEM501 4.3 27.8 1.0
C2C D:HEM501 4.3 28.9 1.0
N D:GLY265 4.7 26.1 1.0
C D:ALA264 4.7 26.2 1.0
CA D:ALA264 4.8 26.9 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

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