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Calcium in PDB 1xh2: Structure of the N298S Variant of Human Pancreatic Alpha-Amylase Complexed with Chloride and Acarbose

Enzymatic activity of Structure of the N298S Variant of Human Pancreatic Alpha-Amylase Complexed with Chloride and Acarbose

All present enzymatic activity of Structure of the N298S Variant of Human Pancreatic Alpha-Amylase Complexed with Chloride and Acarbose:
3.2.1.1;

Protein crystallography data

The structure of Structure of the N298S Variant of Human Pancreatic Alpha-Amylase Complexed with Chloride and Acarbose, PDB code: 1xh2 was solved by R.Maurus, A.Begum, H.H.Kuo, A.Racaza, S.Numao, C.M.Overall, S.G.Withers, G.D.Brayer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 2.20
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 53.135, 69.392, 132.447, 90.00, 90.00, 90.00
R / Rfree (%) 15.6 / 21.4

Other elements in 1xh2:

The structure of Structure of the N298S Variant of Human Pancreatic Alpha-Amylase Complexed with Chloride and Acarbose also contains other interesting chemical elements:

Chlorine (Cl) 1 atom

Calcium Binding Sites:

The binding sites of Calcium atom in the Structure of the N298S Variant of Human Pancreatic Alpha-Amylase Complexed with Chloride and Acarbose (pdb code 1xh2). 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 the N298S Variant of Human Pancreatic Alpha-Amylase Complexed with Chloride and Acarbose, PDB code: 1xh2:

Calcium binding site 1 out of 1 in 1xh2

Go back to Calcium Binding Sites List in 1xh2
Calcium binding site 1 out of 1 in the Structure of the N298S Variant of Human Pancreatic Alpha-Amylase Complexed with Chloride and Acarbose


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Structure of the N298S Variant of Human Pancreatic Alpha-Amylase Complexed with Chloride and Acarbose within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca498

b:23.1
occ:1.00
 OD1 A:ASN100 2.6 21.6 1.0
O A:HIS201 2.6 21.5 1.0
O A:ARG158 2.6 24.3 1.0
OD2 A:ASP167 2.6 22.1 1.0
OD1 A:ASP167 2.7 21.9 1.0
O A:HOH845 2.7 50.1 1.0
O A:HOH514 2.8 29.2 1.0
O A:HOH844 2.9 37.4 1.0
CG A:ASP167 3.0 22.3 1.0
CG A:ASN100 3.6 21.9 1.0
C A:ARG158 3.7 25.0 1.0
C A:HIS201 3.7 21.9 1.0
ND2 A:ASN100 4.1 20.8 1.0
CB A:HIS201 4.1 21.9 1.0
CA A:ARG158 4.2 24.7 1.0
O A:ASN100 4.4 22.7 1.0
CA A:HIS201 4.4 21.7 1.0
CB A:ASP167 4.5 22.4 1.0
O A:CYS160 4.5 25.6 1.0
O A:HOH587 4.6 27.7 1.0
N A:MET202 4.6 21.6 1.0
ND2 A:ASN137 4.6 27.8 1.0
N A:ASP159 4.7 25.3 1.0
CA A:MET202 4.7 21.4 1.0
CG A:MET202 4.8 22.0 1.0
O A:LEU168 4.8 22.8 1.0
O A:VAL157 4.9 25.4 1.0
CB A:ASN100 4.9 21.5 1.0
O A:HOH508 4.9 24.0 1.0
CA A:ASP159 5.0 25.5 1.0

Reference:

R.Maurus, A.Begum, H.H.Kuo, A.Racaza, S.Numao, C.Andersen, J.W.Tams, J.Vind, C.M.Overall, S.G.Withers, G.D.Brayer. Structural and Mechanistic Studies of Chloride Induced Activation of Human Pancreatic Alpha-Amylase Protein Sci. V. 14 743 2005.
ISSN: ISSN 0961-8368
PubMed: 15722449
DOI: 10.1110/PS.041079305
Page generated: Fri Jul 12 07:32:13 2024

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