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Magnesium in PDB 6d3k: Crystal Structure of Unphosphorylated Human Pkr Kinase Domain in Complex with AdpEnzymatic activity of Crystal Structure of Unphosphorylated Human Pkr Kinase Domain in Complex with Adp
All present enzymatic activity of Crystal Structure of Unphosphorylated Human Pkr Kinase Domain in Complex with Adp:
2.7.10.2; 2.7.11.1; Protein crystallography data
The structure of Crystal Structure of Unphosphorylated Human Pkr Kinase Domain in Complex with Adp, PDB code: 6d3k
was solved by
H.Erlandsen,
C.B.Mayo,
V.L.Robinson,
J.L.Cole,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Crystal Structure of Unphosphorylated Human Pkr Kinase Domain in Complex with Adp
(pdb code 6d3k). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 3 binding sites of Magnesium where determined in the Crystal Structure of Unphosphorylated Human Pkr Kinase Domain in Complex with Adp, PDB code: 6d3k: Jump to Magnesium binding site number: 1; 2; 3; Magnesium binding site 1 out of 3 in 6d3kGo back to Magnesium Binding Sites List in 6d3k
Magnesium binding site 1 out
of 3 in the Crystal Structure of Unphosphorylated Human Pkr Kinase Domain in Complex with Adp
Mono view Stereo pair view
Magnesium binding site 2 out of 3 in 6d3kGo back to Magnesium Binding Sites List in 6d3k
Magnesium binding site 2 out
of 3 in the Crystal Structure of Unphosphorylated Human Pkr Kinase Domain in Complex with Adp
Mono view Stereo pair view
Magnesium binding site 3 out of 3 in 6d3kGo back to Magnesium Binding Sites List in 6d3k
Magnesium binding site 3 out
of 3 in the Crystal Structure of Unphosphorylated Human Pkr Kinase Domain in Complex with Adp
Mono view Stereo pair view
Reference:
C.B.Mayo,
H.Erlandsen,
D.J.Mouser,
A.G.Feinstein,
V.L.Robinson,
E.R.May,
J.L.Cole.
Structural Basis of Protein Kinase R Autophosphorylation. Biochemistry V. 58 2967 2019.
Page generated: Mon Dec 14 22:33:21 2020
ISSN: ISSN 0006-2960 PubMed: 31246429 DOI: 10.1021/ACS.BIOCHEM.9B00161 |
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