Iron in PDB 7ah5: Crystal Structure of Indoleamine 2,3-Dioxygenase 1 (IDO1) in Complex with Ferric Heme and Mmg-0706

Enzymatic activity of Crystal Structure of Indoleamine 2,3-Dioxygenase 1 (IDO1) in Complex with Ferric Heme and Mmg-0706

All present enzymatic activity of Crystal Structure of Indoleamine 2,3-Dioxygenase 1 (IDO1) in Complex with Ferric Heme and Mmg-0706:
1.13.11.52;

Protein crystallography data

The structure of Crystal Structure of Indoleamine 2,3-Dioxygenase 1 (IDO1) in Complex with Ferric Heme and Mmg-0706, PDB code: 7ah5 was solved by U.F.Roehrig, A.Reynaud, F.Pojer, O.Michielin, V.Zoete, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 46.55 / 2.90
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 84.988, 93.106, 130.36, 90, 90, 90
R / Rfree (%) 23.1 / 29.2

Other elements in 7ah5:

The structure of Crystal Structure of Indoleamine 2,3-Dioxygenase 1 (IDO1) in Complex with Ferric Heme and Mmg-0706 also contains other interesting chemical elements:

Chlorine (Cl) 4 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of Indoleamine 2,3-Dioxygenase 1 (IDO1) in Complex with Ferric Heme and Mmg-0706 (pdb code 7ah5). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Crystal Structure of Indoleamine 2,3-Dioxygenase 1 (IDO1) in Complex with Ferric Heme and Mmg-0706, PDB code: 7ah5:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 7ah5

Go back to Iron Binding Sites List in 7ah5
Iron binding site 1 out of 2 in the Crystal Structure of Indoleamine 2,3-Dioxygenase 1 (IDO1) in Complex with Ferric Heme and Mmg-0706


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 Indoleamine 2,3-Dioxygenase 1 (IDO1) in Complex with Ferric Heme and Mmg-0706 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe501

b:62.2
occ:1.00
FE A:HEM501 0.0 62.2 1.0
N03 A:RCQ502 2.0 57.4 0.8
ND A:HEM501 2.0 54.7 1.0
NA A:HEM501 2.0 55.8 1.0
NB A:HEM501 2.1 60.6 1.0
NC A:HEM501 2.1 51.0 1.0
NE2 A:HIS346 2.5 58.7 1.0
N02 A:RCQ502 2.8 53.3 0.8
C4A A:HEM501 3.0 62.5 1.0
C1A A:HEM501 3.0 62.6 1.0
C08 A:RCQ502 3.0 57.8 0.8
C4D A:HEM501 3.0 58.9 1.0
C1D A:HEM501 3.0 57.0 1.0
C1B A:HEM501 3.1 60.4 1.0
C4C A:HEM501 3.1 54.2 1.0
C4B A:HEM501 3.1 54.0 1.0
C1C A:HEM501 3.2 51.5 1.0
CD2 A:HIS346 3.2 57.0 1.0
CHA A:HEM501 3.4 61.5 1.0
CHB A:HEM501 3.4 59.3 1.0
CHD A:HEM501 3.4 55.5 1.0
CHC A:HEM501 3.5 50.6 1.0
CE1 A:HIS346 3.6 61.5 1.0
C07 A:RCQ502 4.0 54.8 0.8
N04 A:RCQ502 4.1 57.8 0.8
C3A A:HEM501 4.1 64.6 1.0
C2A A:HEM501 4.2 63.8 1.0
C2D A:HEM501 4.2 59.9 1.0
C3D A:HEM501 4.2 58.7 1.0
C2B A:HEM501 4.3 64.2 1.0
C3C A:HEM501 4.3 58.8 1.0
C3B A:HEM501 4.3 58.6 1.0
C2C A:HEM501 4.4 56.1 1.0
CG A:HIS346 4.4 67.3 1.0
ND1 A:HIS346 4.5 71.2 1.0
CB A:ALA264 4.6 50.0 1.0

Iron binding site 2 out of 2 in 7ah5

Go back to Iron Binding Sites List in 7ah5
Iron binding site 2 out of 2 in the Crystal Structure of Indoleamine 2,3-Dioxygenase 1 (IDO1) in Complex with Ferric Heme and Mmg-0706


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 Indoleamine 2,3-Dioxygenase 1 (IDO1) in Complex with Ferric Heme and Mmg-0706 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe501

b:56.7
occ:0.93
FE B:HEM501 0.0 56.7 0.9
N03 B:RCQ502 1.9 55.7 0.9
NC B:HEM501 2.0 54.6 0.9
ND B:HEM501 2.0 53.3 0.9
NB B:HEM501 2.0 58.9 0.9
NA B:HEM501 2.1 52.6 0.9
NE2 B:HIS346 2.5 51.9 1.0
C08 B:RCQ502 2.8 51.8 0.9
N02 B:RCQ502 2.9 57.2 0.9
C4C B:HEM501 3.0 55.4 0.9
C1D B:HEM501 3.0 51.6 0.9
C4A B:HEM501 3.0 51.1 0.9
C1C B:HEM501 3.0 56.9 0.9
C1B B:HEM501 3.1 55.6 0.9
C4B B:HEM501 3.1 60.7 0.9
C1A B:HEM501 3.1 53.8 0.9
C4D B:HEM501 3.1 52.0 0.9
CD2 B:HIS346 3.3 55.6 1.0
CHD B:HEM501 3.4 54.6 0.9
CHB B:HEM501 3.4 54.5 0.9
CHC B:HEM501 3.5 57.5 0.9
CHA B:HEM501 3.5 51.7 0.9
CE1 B:HIS346 3.5 49.2 1.0
N04 B:RCQ502 3.9 54.2 0.9
C07 B:RCQ502 3.9 57.4 0.9
C3C B:HEM501 4.2 53.5 0.9
C2C B:HEM501 4.2 54.7 0.9
C3A B:HEM501 4.2 54.0 0.9
C2D B:HEM501 4.3 49.2 0.9
C2A B:HEM501 4.3 56.3 0.9
C2B B:HEM501 4.3 58.9 0.9
C3B B:HEM501 4.3 63.3 0.9
C3D B:HEM501 4.3 48.9 0.9
CG B:HIS346 4.5 59.9 1.0
ND1 B:HIS346 4.5 58.7 1.0
CB B:ALA264 4.6 54.8 1.0

Reference:

U.F.Rohrig, S.R.Majjigapu, A.Reynaud, F.Pojer, N.Dilek, P.Reichenbach, K.Ascencao, M.Irving, G.Coukos, P.Vogel, O.Michielin, V.Zoete. Azole-Based Indoleamine 2,3-Dioxygenase 1 (IDO1) Inhibitors J.Med.Chem. 2021.
ISSN: ISSN 0022-2623
DOI: 10.1021/ACS.JMEDCHEM.0C01968
Page generated: Wed Mar 3 14:01:10 2021

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