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Chlorine in PDB 7nge: Crystal Structure of L-Trp/Indoleamine 2,3-Dioxygenagse 1 (HIDO1) Complex with the Jk-Loop Refined in the Closed ConformationEnzymatic activity of Crystal Structure of L-Trp/Indoleamine 2,3-Dioxygenagse 1 (HIDO1) Complex with the Jk-Loop Refined in the Closed Conformation
All present enzymatic activity of Crystal Structure of L-Trp/Indoleamine 2,3-Dioxygenagse 1 (HIDO1) Complex with the Jk-Loop Refined in the Closed Conformation:
1.13.11.52; Protein crystallography data
The structure of Crystal Structure of L-Trp/Indoleamine 2,3-Dioxygenagse 1 (HIDO1) Complex with the Jk-Loop Refined in the Closed Conformation, PDB code: 7nge
was solved by
M.Mirgaux,
J.Wouters,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 7nge:
The structure of Crystal Structure of L-Trp/Indoleamine 2,3-Dioxygenagse 1 (HIDO1) Complex with the Jk-Loop Refined in the Closed Conformation also contains other interesting chemical elements:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Crystal Structure of L-Trp/Indoleamine 2,3-Dioxygenagse 1 (HIDO1) Complex with the Jk-Loop Refined in the Closed Conformation
(pdb code 7nge). This binding sites where shown within
5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Crystal Structure of L-Trp/Indoleamine 2,3-Dioxygenagse 1 (HIDO1) Complex with the Jk-Loop Refined in the Closed Conformation, PDB code: 7nge: Chlorine binding site 1 out of 1 in 7ngeGo back to Chlorine Binding Sites List in 7nge
Chlorine binding site 1 out
of 1 in the Crystal Structure of L-Trp/Indoleamine 2,3-Dioxygenagse 1 (HIDO1) Complex with the Jk-Loop Refined in the Closed Conformation
Mono view Stereo pair view
Reference:
M.Mirgaux,
L.Leherte,
J.Wouters.
Temporary Intermediates of L-Trp Along the Reaction Pathway of Human Indoleamine 2,3-Dioxygenase 1 and Identification of An Exo Site International Journal of 2021TRYPTOPHAN Research.
Page generated: Thu Mar 31 02:37:31 2022
DOI: 10.1177/11786469211052964 |
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