Chlorine in PDB 5my9: Crystal Structure of Human 14-3-3 Sigma in Complex with LRRK2 Peptide PS935

Enzymatic activity of Crystal Structure of Human 14-3-3 Sigma in Complex with LRRK2 Peptide PS935

All present enzymatic activity of Crystal Structure of Human 14-3-3 Sigma in Complex with LRRK2 Peptide PS935:
2.7.11.1;

Protein crystallography data

The structure of Crystal Structure of Human 14-3-3 Sigma in Complex with LRRK2 Peptide PS935, PDB code: 5my9 was solved by L.M.Stevers, R.M.J.M.De Vries, C.Ottmann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	45.46 / 1.33
*Space group*	C 2 2 2₁
*Cell size a, b, c (Å), α, β, γ (°)*	82.291, 112.030, 62.430, 90.00, 90.00, 90.00
*R / R_free (%)*	18.7 / 20.1

Other elements in 5my9:

The structure of Crystal Structure of Human 14-3-3 Sigma in Complex with LRRK2 Peptide PS935 also contains other interesting chemical elements:

Calcium

(Ca)

3 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Human 14-3-3 Sigma in Complex with LRRK2 Peptide PS935 (pdb code 5my9). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Crystal Structure of Human 14-3-3 Sigma in Complex with LRRK2 Peptide PS935, PDB code: 5my9:

Chlorine binding site 1 out of 1 in 5my9

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Chlorine Binding Sites List in 5my9

Chlorine binding site 1 out of 1 in the Crystal Structure of Human 14-3-3 Sigma in Complex with LRRK2 Peptide PS935

Mono view

Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Human 14-3-3 Sigma in Complex with LRRK2 Peptide PS935 within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Cl304 b:17.6 occ:1.00	O	A:HOH717	3.0	24.8	1.0
	O	A:HOH764	3.1	20.7	1.0
	CA	A:TYR84	3.8	11.7	1.0
	O	A:GLU83	3.9	12.2	1.0
	CD	A:LYS87	3.9	24.0	1.0
	N	A:TYR84	4.0	11.0	1.0
	C	A:GLU83	4.0	11.6	1.0
	CB	A:LYS87	4.1	14.3	1.0
	CD1	A:TYR84	4.1	12.0	1.0
	CB	A:TYR84	4.2	14.1	1.0
	CB	A:GLU83	4.3	12.6	1.0
	CG	A:LYS87	4.5	19.0	1.0
	O	A:HOH457	4.5	21.7	1.0
	CG	A:TYR84	4.6	12.7	1.0
	CE	A:LYS87	4.8	32.2	1.0
	CA	A:GLU83	4.8	12.2	1.0
	O	A:HOH770	5.0	51.9	1.0

Reference:

L.M.Stevers, R.M.De Vries, R.G.Doveston, L.G.Milroy, L.Brunsveld, C.Ottmann. Structural Interface Between LRRK2 and 14-3-3 Protein. Biochem. J. V. 474 1273 2017.
ISSN: ESSN 1470-8728
PubMed: 28202711
DOI: 10.1042/BCJ20161078

Page generated: Sat Jul 12 05:44:44 2025

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