Potassium in PDB 4ihl: Human 14-3-3 Isoform Zeta in Complex with A Diphoyphorylated C-Raf Peptide and Cotylenin A

All present enzymatic activity of Human 14-3-3 Isoform Zeta in Complex with A Diphoyphorylated C-Raf Peptide and Cotylenin A:
2.7.11.1;

The structure of Human 14-3-3 Isoform Zeta in Complex with A Diphoyphorylated C-Raf Peptide and Cotylenin A, PDB code: 4ihl was solved by M.Molzan, C.Ottmann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	49.40 / 2.20
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	72.280, 103.400, 112.580, 90.00, 90.00, 90.00
R / Rfree (%)	20 / 24.3

The binding sites of Potassium atom in the Human 14-3-3 Isoform Zeta in Complex with A Diphoyphorylated C-Raf Peptide and Cotylenin A (pdb code 4ihl). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Human 14-3-3 Isoform Zeta in Complex with A Diphoyphorylated C-Raf Peptide and Cotylenin A, PDB code: 4ihl:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in the Human 14-3-3 Isoform Zeta in Complex with A Diphoyphorylated C-Raf Peptide and Cotylenin A


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Human 14-3-3 Isoform Zeta in Complex with A Diphoyphorylated C-Raf Peptide and Cotylenin A within 5.0Å range: probe atom residue distance (Å) B Occ A:K301 b:76.2 occ:1.00 O P:HOH311 2.5 54.0 1.0 OD2 A:ASP124 3.2 36.1 1.0 CG A:ASP124 4.0 32.6 1.0 NZ A:LYS120 4.1 29.6 1.0 CB A:ASP124 4.2 32.2 1.0 CE2 A:TYR125 4.2 33.0 1.0 O A:HOH513 4.2 39.7 1.0 OH A:TYR128 4.3 30.5 1.0 CD A:LYS49 4.4 47.3 1.0 O P:HOH310 4.4 40.3 1.0 O A:HOH443 4.5 42.8 1.0 OAJ A:1F5302 4.6 42.6 1.0 CG A:MET121 4.6 46.0 1.0 CB A:LYS49 4.7 30.4 1.0 CG A:LYS49 4.7 34.5 1.0 OG A:SER45 4.7 36.6 1.0 CAK A:1F5302 4.7 32.3 1.0 OH A:TYR125 4.7 34.2 1.0 CZ A:TYR125 4.9 38.3 1.0 CE2 A:TYR128 5.0 28.2 1.0 CD2 A:TYR125 5.0 33.0 1.0

Potassium binding site 2 out of 2 in the Human 14-3-3 Isoform Zeta in Complex with A Diphoyphorylated C-Raf Peptide and Cotylenin A


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Human 14-3-3 Isoform Zeta in Complex with A Diphoyphorylated C-Raf Peptide and Cotylenin A within 5.0Å range: probe atom residue distance (Å) B Occ B:K301 b:70.0 occ:1.00 O P:HOH313 2.5 47.5 1.0 OD2 B:ASP124 3.1 41.5 1.0 CG B:ASP124 3.9 42.5 1.0 CB B:ASP124 4.1 35.5 1.0 OH B:TYR128 4.2 35.4 1.0 NZ B:LYS120 4.2 35.3 1.0 O P:HOH302 4.2 41.7 1.0 O B:HOH417 4.3 43.3 1.0 CE2 B:TYR125 4.3 38.8 1.0 CD B:LYS49 4.3 58.0 1.0 O B:HOH490 4.5 42.3 1.0 CAK B:1F5302 4.5 28.3 1.0 OG B:SER45 4.6 40.5 1.0 CB B:LYS49 4.7 35.8 1.0 CG B:LYS49 4.7 43.0 1.0 OG1 P:THR234 4.8 32.2 0.5 ND2 B:ASN173 4.8 29.6 1.0 OAJ B:1F5302 4.8 39.8 1.0 OH B:TYR125 4.9 39.3 1.0 CG B:MET121 4.9 51.3 1.0 OD1 B:ASP124 5.0 38.5 1.0 NZ B:LYS49 5.0 61.7 1.0

M.Molzan, S.Kasper, L.Roglin, M.Skwarczynska, T.Sassa, T.Inoue, F.Breitenbuecher, J.Ohkanda, N.Kato, M.Schuler, C.Ottmann. Stabilization of Physical Raf/14-3-3 Interaction By Cotylenin A As Treatment Strategy For Ras Mutant Cancers. Acs Chem.Biol. V. 8 1869 2013.
ISSN: ISSN 1554-8929
PubMed: 23808890
DOI: 10.1021/CB4003464