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Iron in PDB 6r63: Crystal Structure of Indoleamine 2,3-Dioxygenase 1 (IDO1) in Complex with Ferric Heme and Mmg-0358Enzymatic activity of Crystal Structure of Indoleamine 2,3-Dioxygenase 1 (IDO1) in Complex with Ferric Heme and Mmg-0358
All present enzymatic activity of Crystal Structure of Indoleamine 2,3-Dioxygenase 1 (IDO1) in Complex with Ferric Heme and Mmg-0358:
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-0358, PDB code: 6r63
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:
Other elements in 6r63:
The structure of Crystal Structure of Indoleamine 2,3-Dioxygenase 1 (IDO1) in Complex with Ferric Heme and Mmg-0358 also contains other interesting chemical elements:
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-0358
(pdb code 6r63). 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-0358, PDB code: 6r63: Jump to Iron binding site number: 1; 2; Iron binding site 1 out of 2 in 6r63Go back to Iron Binding Sites List in 6r63
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-0358
Mono view Stereo pair view
Iron binding site 2 out of 2 in 6r63Go back to Iron Binding Sites List in 6r63
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-0358
Mono view Stereo pair view
Reference:
U.F.Rohrig,
A.Reynaud,
S.R.Majjigapu,
P.Vogel,
F.Pojer,
V.Zoete.
Inhibition Mechanisms of Indoleamine 2,3-Dioxygenase 1 (IDO1). J.Med.Chem. V. 62 8784 2019.
Page generated: Sun Dec 13 16:58:40 2020
ISSN: ISSN 0022-2623 PubMed: 31525930 DOI: 10.1021/ACS.JMEDCHEM.9B00942 |
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