Chlorine in PDB 4x0n: Porcine Pancreatic Alpha-Amylase in Complex with Helianthamide, A Novel Proteinaceous Inhibitor

Enzymatic activity of Porcine Pancreatic Alpha-Amylase in Complex with Helianthamide, A Novel Proteinaceous Inhibitor

All present enzymatic activity of Porcine Pancreatic Alpha-Amylase in Complex with Helianthamide, A Novel Proteinaceous Inhibitor:
3.2.1.1;

Protein crystallography data

The structure of Porcine Pancreatic Alpha-Amylase in Complex with Helianthamide, A Novel Proteinaceous Inhibitor, PDB code: 4x0n was solved by L.K.Williams, G.D.Brayer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	46.89 / 2.60
*Space group*	P 2₁ 2₁ 2₁
*Cell size a, b, c (Å), α, β, γ (°)*	43.750, 103.280, 111.896, 90.00, 90.00, 90.00
*R / R_free (%)*	18.2 / 22.6

Other elements in 4x0n:

The structure of Porcine Pancreatic Alpha-Amylase in Complex with Helianthamide, A Novel Proteinaceous Inhibitor also contains other interesting chemical elements:

Calcium

(Ca)

1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Porcine Pancreatic Alpha-Amylase in Complex with Helianthamide, A Novel Proteinaceous Inhibitor (pdb code 4x0n). 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 Porcine Pancreatic Alpha-Amylase in Complex with Helianthamide, A Novel Proteinaceous Inhibitor, PDB code: 4x0n:

Chlorine binding site 1 out of 1 in 4x0n

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Chlorine Binding Sites List in 4x0n

Chlorine binding site 1 out of 1 in the Porcine Pancreatic Alpha-Amylase in Complex with Helianthamide, A Novel Proteinaceous Inhibitor

Mono view

Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Porcine Pancreatic Alpha-Amylase in Complex with Helianthamide, A Novel Proteinaceous Inhibitor within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Cl501 b:10.0 occ:1.00	NH1	A:ARG195	2.5	20.7	1.0
	NH2	A:ARG337	3.2	10.4	1.0
	O	A:HOH684	3.2	11.3	1.0
	NH1	A:ARG337	3.4	15.9	1.0
	ND2	A:ASN298	3.5	10.0	1.0
	CZ	A:ARG195	3.7	15.2	1.0
	CZ	A:ARG337	3.7	15.5	1.0
	CG2	A:THR254	4.0	12.1	1.0
	CG	A:GLU233	4.1	15.6	1.0
	CZ	A:PHE256	4.1	12.5	1.0
	CD	A:ARG195	4.4	13.7	1.0
	CG	A:ASN298	4.4	11.8	1.0
	NE	A:ARG195	4.4	15.9	1.0
	CB	A:ASN298	4.4	12.7	1.0
	CB	A:GLU233	4.5	14.6	1.0
	NH2	A:ARG195	4.5	16.8	1.0
	OE2	A:GLU233	4.6	12.3	1.0
	CD	A:GLU233	4.7	17.4	1.0
	CZ	A:PHE295	4.7	11.3	1.0
	CE1	A:PHE256	4.8	12.8	1.0
	O	A:HOH768	4.8	13.0	1.0
	CE1	A:PHE295	4.9	11.4	1.0
	CE2	A:PHE256	4.9	10.2	1.0
	CB	A:THR254	4.9	12.9	1.0
	CE1	A:HIS299	5.0	13.1	1.0

Reference:

C.Tysoe, L.K.Williams, R.Keyzers, N.T.Nguyen, A.Aguda, X.Zhang, C.A.Tarling, R.J.Andersen, G.D.Brayer, S.G.Withers. Structural Templating and Guided Refolding of the Potent Naturally Occurring Peptide Helianthamide Within the Active Site of Amylase, A Diabetes and Obesity Therapeutic Target To Be Published.

Page generated: Fri Jul 11 22:42:57 2025

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