Calcium in PDB 1hx0: Structure of Pig Pancreatic Alpha-Amylase Complexed with the "Truncate" Acarbose Molecule (Pseudotrisaccharide)

Enzymatic activity of Structure of Pig Pancreatic Alpha-Amylase Complexed with the "Truncate" Acarbose Molecule (Pseudotrisaccharide)

All present enzymatic activity of Structure of Pig Pancreatic Alpha-Amylase Complexed with the "Truncate" Acarbose Molecule (Pseudotrisaccharide):
3.2.1.1;

Protein crystallography data

The structure of Structure of Pig Pancreatic Alpha-Amylase Complexed with the "Truncate" Acarbose Molecule (Pseudotrisaccharide), PDB code: 1hx0 was solved by M.Qian, F.Payan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	35.00 / 1.38
*Space group*	P 2₁ 2₁ 2₁
*Cell size a, b, c (Å), α, β, γ (°)*	69.280, 113.550, 117.160, 90.00, 90.00, 90.00
*R / R_free (%)*	10.8 / 13

Other elements in 1hx0:

The structure of Structure of Pig Pancreatic Alpha-Amylase Complexed with the "Truncate" Acarbose Molecule (Pseudotrisaccharide) also contains other interesting chemical elements:

Chlorine

(Cl)

4 atoms

Calcium Binding Sites:

The binding sites of Calcium atom in the Structure of Pig Pancreatic Alpha-Amylase Complexed with the "Truncate" Acarbose Molecule (Pseudotrisaccharide) (pdb code 1hx0). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Structure of Pig Pancreatic Alpha-Amylase Complexed with the "Truncate" Acarbose Molecule (Pseudotrisaccharide), PDB code: 1hx0:

Calcium binding site 1 out of 1 in 1hx0

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Calcium Binding Sites List in 1hx0

Calcium binding site 1 out of 1 in the Structure of Pig Pancreatic Alpha-Amylase Complexed with the "Truncate" Acarbose Molecule (Pseudotrisaccharide)

Mono view

Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Structure of Pig Pancreatic Alpha-Amylase Complexed with the "Truncate" Acarbose Molecule (Pseudotrisaccharide) within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Ca500 b:14.4 occ:1.00	OD1	A:ASN100	2.3	14.6	1.0
	O	A:ARG158	2.4	15.1	1.0
	O	A:HIS201	2.4	13.6	1.0
	O	A:HOH6023	2.5	14.7	1.0
	OD2	A:ASP167	2.5	15.7	1.0
	O	A:HOH6017	2.5	15.8	1.0
	O	A:HOH6031	2.5	17.9	1.0
	OD1	A:ASP167	2.6	16.4	1.0
	CG	A:ASP167	2.8	14.9	1.0
	C	A:ARG158	3.4	13.7	1.0
	CG	A:ASN100	3.4	12.2	1.0
	C	A:HIS201	3.6	12.7	1.0
	ND2	A:ASN100	3.8	15.0	1.0
	CA	A:ARG158	4.1	14.7	1.0
	CB	A:HIS201	4.2	13.2	1.0
	CB	A:ASP167	4.3	14.6	1.0
	O	A:ASN100	4.4	14.2	1.0
	CA	A:HIS201	4.4	13.0	1.0
	N	A:ASP159	4.4	15.4	1.0
	O	A:HOH6204	4.4	18.9	1.0
	ND2	A:ASN137	4.5	20.6	0.5
	N	A:MET202	4.5	14.0	1.0
	O	A:CYS160	4.5	18.2	1.0
	CG	A:MET202	4.6	17.9	1.0
	OD1	A:ASN137	4.6	16.1	0.5
	O	A:VAL157	4.7	15.3	1.0
	CA	A:MET202	4.7	13.6	1.0
	CB	A:ASN100	4.7	13.3	1.0
	CA	A:ASP159	4.7	15.5	1.0
	O	A:LEU168	4.8	15.7	1.0
	CB	A:ARG158	4.9	16.4	0.6
	CB	A:ARG158	5.0	16.1	0.4

Reference:

M.Qian, V.Nahoum, J.Bonicel, H.Bischoff, B.Henrissat, F.Payan. Enzyme-Catalyzed Condensation Reaction in A Mammalian Alpha-Amylase. High-Resolution Structural Analysis of An Enzyme-Inhibitor Complex Biochemistry V. 40 7700 2001.
ISSN: ISSN 0006-2960
PubMed: 11412124
DOI: 10.1021/BI0102050

Page generated: Sat Dec 12 03:00:03 2020

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