Chlorine in PDB 5myc: Crystal Structure of Human 14-3-3 Sigma in Complex with LRRK2 Peptide PS910

Enzymatic activity of Crystal Structure of Human 14-3-3 Sigma in Complex with LRRK2 Peptide PS910

All present enzymatic activity of Crystal Structure of Human 14-3-3 Sigma in Complex with LRRK2 Peptide PS910:
2.7.11.1;

Protein crystallography data

The structure of Crystal Structure of Human 14-3-3 Sigma in Complex with LRRK2 Peptide PS910, PDB code: 5myc 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)*	41.85 / 1.46
*Space group*	C 2 2 2₁
*Cell size a, b, c (Å), α, β, γ (°)*	82.517, 112.411, 62.689, 90.00, 90.00, 90.00
*R / R_free (%)*	16.6 / 18.9

Other elements in 5myc:

The structure of Crystal Structure of Human 14-3-3 Sigma in Complex with LRRK2 Peptide PS910 also contains other interesting chemical elements:

Calcium	(Ca)	2 atoms
Sodium	(Na)	1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Human 14-3-3 Sigma in Complex with LRRK2 Peptide PS910 (pdb code 5myc). 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 PS910, PDB code: 5myc:

Chlorine binding site 1 out of 1 in 5myc

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Chlorine Binding Sites List in 5myc

Chlorine binding site 1 out of 1 in the Crystal Structure of Human 14-3-3 Sigma in Complex with LRRK2 Peptide PS910

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 PS910 within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Cl303 b:22.1 occ:1.00	O	A:HOH735	3.0	29.1	1.0
	O	A:HOH652	3.0	25.2	1.0
	CD	A:LYS87	3.7	20.4	0.3
	CA	A:TYR84	3.9	11.5	1.0
	O	A:GLU83	3.9	13.3	1.0
	CD	A:LYS87	3.9	20.8	0.7
	CB	A:LYS87	4.0	15.4	0.3
	CB	A:LYS87	4.0	14.4	0.7
	C	A:GLU83	4.1	12.4	1.0
	CD1	A:TYR84	4.1	12.5	1.0
	N	A:TYR84	4.1	11.3	1.0
	CB	A:TYR84	4.3	11.8	1.0
	CG	A:LYS87	4.4	17.1	0.3
	CB	A:GLU83	4.4	13.9	1.0
	CG	A:LYS87	4.5	16.8	0.7
	O	A:HOH475	4.6	23.7	1.0
	CG	A:TYR84	4.6	10.9	1.0
	CE	A:LYS87	4.7	23.2	0.3
	NZ	A:LYS87	4.9	22.2	0.3
	CA	A:GLU83	4.9	13.7	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: Fri Jul 26 13:02:42 2024

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