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Potassium in PDB 5li1: Structure of A PAR3-Inhibitory Peptide Bound to Pkciota Core Kinase Domain

Enzymatic 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:

Resolution Low / High (Å) 41.01 / 2.00
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 82.030, 82.030, 90.790, 90.00, 90.00, 120.00
R / Rfree (%) 15 / 21.7

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:

Magnesium (Mg) 2 atoms

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 5li1

Go 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

A full contact list of Potassium with other atoms in the K binding site number 1 of Structure of A PAR3-Inhibitory Peptide Bound to Pkciota Core Kinase Domain within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K603

b:38.9
occ:1.00
 O A:HIS312 2.5 16.0 1.0
O A:LEU315 2.6 13.3 1.0
O A:HOH815 2.7 46.0 1.0
O A:ALA309 2.9 22.5 1.0
OE2 A:GLU333 3.6 23.8 1.0
C A:HIS312 3.6 16.0 1.0
C A:LEU315 3.7 11.6 1.0
C A:ALA309 3.9 27.5 1.0
N A:GLY317 4.1 12.7 1.0
CA A:SER310 4.1 39.0 1.0
O A:SER310 4.1 46.5 1.0
C A:SER310 4.2 34.3 1.0
N A:HIS312 4.3 21.4 1.0
N A:LEU315 4.4 16.0 1.0
N A:SER310 4.4 26.3 1.0
CA A:GLY317 4.5 22.1 1.0
CA A:PRO313 4.5 19.3 1.0
C A:PRO313 4.5 33.0 1.0
O A:PRO313 4.5 21.3 1.0
N A:PRO313 4.5 19.6 1.0
CA A:LEU315 4.5 15.8 1.0
CA A:HIS312 4.6 16.2 1.0
C A:VAL316 4.6 17.5 1.0
N A:VAL316 4.7 15.8 1.0
CD A:GLU333 4.7 49.0 1.0
CA A:VAL316 4.8 10.7 1.0
CB A:LEU315 4.8 19.6 1.0
NZ A:LYS393 4.8 25.4 1.0
N A:ASN311 4.9 22.3 1.0

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.
ISSN: ISSN 1534-5807
PubMed: 27554858
DOI: 10.1016/J.DEVCEL.2016.07.018
Page generated: Sat Aug 9 09:30:38 2025

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