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Atomistry » Potassium » PDB 5ksd-5mq0 » 5li1 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Potassium » PDB 5ksd-5mq0 » 5li1 » |
Potassium in PDB 5li1: Structure of A PAR3-Inhibitory Peptide Bound to Pkciota Core Kinase DomainEnzymatic activity of Structure of A PAR3-Inhibitory Peptide Bound to Pkciota Core Kinase Domain
All present enzymatic activity of Structure of A PAR3-Inhibitory Peptide Bound to Pkciota Core Kinase Domain:
2.7.11.13; Protein crystallography data
The structure of Structure of A PAR3-Inhibitory Peptide Bound to Pkciota Core Kinase Domain, PDB code: 5li1
was solved by
E.V.Soriano,
A.G.Purkiss,
N.Q.Mcdonald,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 5li1:
The structure of Structure of A PAR3-Inhibitory Peptide Bound to Pkciota Core Kinase Domain also contains other interesting chemical elements:
Potassium Binding Sites:
The binding sites of Potassium atom in the Structure of A PAR3-Inhibitory Peptide Bound to Pkciota Core Kinase Domain
(pdb code 5li1). This binding sites where shown within
5.0 Angstroms radius around Potassium atom.
In total only one binding site of Potassium was determined in the Structure of A PAR3-Inhibitory Peptide Bound to Pkciota Core Kinase Domain, PDB code: 5li1: Potassium binding site 1 out of 1 in 5li1Go back to Potassium Binding Sites List in 5li1
Potassium binding site 1 out
of 1 in the Structure of A PAR3-Inhibitory Peptide Bound to Pkciota Core Kinase Domain
Mono view Stereo pair view
Reference:
E.V.Soriano,
M.E.Ivanova,
G.Fletcher,
P.Riou,
P.P.Knowles,
K.Barnouin,
A.Purkiss,
B.Kostelecky,
P.Saiu,
M.Linch,
A.Elbediwy,
S.Kjr,
N.O'reilly,
A.P.Snijders,
P.J.Parker,
B.J.Thompson,
N.Q.Mcdonald.
Apkc Inhibition By PAR3 CR3 Flanking Regions Controls Substrate Access and Underpins Apical-Junctional Polarization. Dev.Cell V. 38 384 2016.
Page generated: Mon Dec 14 00:03:51 2020
ISSN: ISSN 1534-5807 PubMed: 27554858 DOI: 10.1016/J.DEVCEL.2016.07.018 |
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