Chlorine in PDB 4nm3: Crystal Structure of Gsk-3/Axin Complex Bound to Phosphorylated N- Terminal Auto-Inhibitory PS9 Peptide

Enzymatic activity of Crystal Structure of Gsk-3/Axin Complex Bound to Phosphorylated N- Terminal Auto-Inhibitory PS9 Peptide

All present enzymatic activity of Crystal Structure of Gsk-3/Axin Complex Bound to Phosphorylated N- Terminal Auto-Inhibitory PS9 Peptide:
2.7.11.1; 2.7.11.26;

Protein crystallography data

The structure of Crystal Structure of Gsk-3/Axin Complex Bound to Phosphorylated N- Terminal Auto-Inhibitory PS9 Peptide, PDB code: 4nm3 was solved by M.L.-H.Chu, J.L.Stamos, M.D.Enos, N.Shah, W.I.Weis, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	38.96 / 2.10
*Space group*	P 6₁ 2 2
*Cell size a, b, c (Å), α, β, γ (°)*	81.032, 81.032, 281.085, 90.00, 90.00, 120.00
*R / R_free (%)*	19.4 / 24.2

Other elements in 4nm3:

The structure of Crystal Structure of Gsk-3/Axin Complex Bound to Phosphorylated N- Terminal Auto-Inhibitory PS9 Peptide also contains other interesting chemical elements:

Magnesium

(Mg)

2 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Gsk-3/Axin Complex Bound to Phosphorylated N- Terminal Auto-Inhibitory PS9 Peptide (pdb code 4nm3). 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 Gsk-3/Axin Complex Bound to Phosphorylated N- Terminal Auto-Inhibitory PS9 Peptide, PDB code: 4nm3:

Chlorine binding site 1 out of 1 in 4nm3

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Chlorine Binding Sites List in 4nm3

Chlorine binding site 1 out of 1 in the Crystal Structure of Gsk-3/Axin Complex Bound to Phosphorylated N- Terminal Auto-Inhibitory PS9 Peptide

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 Gsk-3/Axin Complex Bound to Phosphorylated N- Terminal Auto-Inhibitory PS9 Peptide within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Cl407 b:71.1 occ:1.00	N	A:LYS297	3.4	45.6	1.0
	CG2	A:ILE296	3.5	44.1	0.5
	CA	A:ILE296	3.6	46.0	0.5
	CA	A:ILE296	3.6	46.0	0.5
	CG2	A:ILE296	3.8	44.1	0.5
	CD1	A:ILE296	3.9	45.5	0.5
	C	A:ILE296	4.0	46.2	1.0
	CB	A:ILE296	4.0	44.5	0.5
	CB	A:ILE296	4.0	44.4	0.5
	CG1	A:ILE296	4.1	45.4	0.5
	O	A:GLN295	4.3	51.3	1.0
	CB	A:LYS297	4.4	52.7	1.0
	CA	A:LYS297	4.4	48.9	1.0
	CG1	A:ILE296	4.6	44.9	0.5
	CG	B:GLN400	4.6	73.4	1.0
	N	A:ILE296	4.7	45.2	1.0
	O	A:LYS297	4.8	46.2	1.0
	CA	B:GLN400	4.9	73.4	1.0
	C	A:GLN295	5.0	49.6	1.0

Reference:

J.L.Stamos, M.L.Chu, M.D.Enos, N.Shah, W.I.Weis. Structural Basis of Gsk-3 Inhibition By N-Terminal Phosphorylation and By the Wnt Receptor LRP6. Elife V. 3 01998 2014.
ISSN: ESSN 2050-084X
PubMed: 24642411

Page generated: Fri Jul 11 19:39:44 2025

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