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Atomistry » Manganese » PDB 5nha-5raa » 5ox6 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Manganese » PDB 5nha-5raa » 5ox6 » |
Manganese in PDB 5ox6: Hif Prolyl Hydroxylase 2 (PHD2/ EGLN1) in Complex with VadadustatEnzymatic activity of Hif Prolyl Hydroxylase 2 (PHD2/ EGLN1) in Complex with Vadadustat
All present enzymatic activity of Hif Prolyl Hydroxylase 2 (PHD2/ EGLN1) in Complex with Vadadustat:
1.14.11.29; Protein crystallography data
The structure of Hif Prolyl Hydroxylase 2 (PHD2/ EGLN1) in Complex with Vadadustat, PDB code: 5ox6
was solved by
R.Chowdhury,
D.Zhang,
C.J.Schofield,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 5ox6:
The structure of Hif Prolyl Hydroxylase 2 (PHD2/ EGLN1) in Complex with Vadadustat also contains other interesting chemical elements:
Manganese Binding Sites:
The binding sites of Manganese atom in the Hif Prolyl Hydroxylase 2 (PHD2/ EGLN1) in Complex with Vadadustat
(pdb code 5ox6). This binding sites where shown within
5.0 Angstroms radius around Manganese atom.
In total only one binding site of Manganese was determined in the Hif Prolyl Hydroxylase 2 (PHD2/ EGLN1) in Complex with Vadadustat, PDB code: 5ox6: Manganese binding site 1 out of 1 in 5ox6Go back to Manganese Binding Sites List in 5ox6
Manganese binding site 1 out
of 1 in the Hif Prolyl Hydroxylase 2 (PHD2/ EGLN1) in Complex with Vadadustat
Mono view Stereo pair view
Reference:
T.L.Yeh,
T.M.Leissing,
M.I.Abboud,
C.C.Thinnes,
O.Atasoylu,
J.P.Holt-Martyn,
D.Zhang,
A.Tumber,
K.Lippl,
C.T.Lohans,
I.K.H.Leung,
H.Morcrette,
I.J.Clifton,
T.D.W.Claridge,
A.Kawamura,
E.Flashman,
X.Lu,
P.J.Ratcliffe,
R.Chowdhury,
C.W.Pugh,
C.J.Schofield.
Molecular and Cellular Mechanisms of Hif Prolyl Hydroxylase Inhibitors in Clinical Trials. Chem Sci V. 8 7651 2017.
Page generated: Tue Dec 15 04:45:50 2020
ISSN: ISSN 2041-6520 PubMed: 29435217 DOI: 10.1039/C7SC02103H |
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