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Calcium in PDB 1xh1: Structure of the N298S Variant of Human Pancreatic Alpha-Amylase Complexed with Chloride

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

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

Protein crystallography data

The structure of Structure of the N298S Variant of Human Pancreatic Alpha-Amylase Complexed with Chloride, PDB code: 1xh1 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 / 2.03
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 52.910, 68.900, 131.770, 90.00, 90.00, 90.00
R / Rfree (%) 16.3 / 20.7

Other elements in 1xh1:

The structure of Structure of the N298S Variant of Human Pancreatic Alpha-Amylase Complexed with Chloride 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 (pdb code 1xh1). 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, PDB code: 1xh1:

Calcium binding site 1 out of 1 in 1xh1

Go back to Calcium Binding Sites List in 1xh1
Calcium binding site 1 out of 1 in the Structure of the N298S Variant of Human Pancreatic Alpha-Amylase Complexed with Chloride


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 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca498

b:18.4
occ:1.00
 OD1 A:ASN100 2.5 16.6 1.0
O A:HIS201 2.6 17.9 1.0
O A:ARG158 2.6 21.2 1.0
OD2 A:ASP167 2.6 17.9 1.0
OD1 A:ASP167 2.7 17.2 1.0
O A:HOH827 2.7 15.8 1.0
O A:HOH826 2.8 19.9 1.0
O A:HOH824 2.8 21.5 1.0
CG A:ASP167 3.0 17.6 1.0
C A:ARG158 3.6 21.0 1.0
CG A:ASN100 3.6 17.3 1.0
C A:HIS201 3.7 18.1 1.0
ND2 A:ASN100 4.1 16.7 1.0
CB A:HIS201 4.2 18.1 1.0
CA A:ARG158 4.2 21.0 1.0
O A:ASN100 4.4 17.5 1.0
CB A:ASP167 4.5 17.8 1.0
CA A:HIS201 4.5 17.8 1.0
O A:CYS160 4.6 21.7 1.0
O A:HOH549 4.6 16.9 1.0
N A:MET202 4.6 17.8 1.0
ND2 A:ASN137 4.6 22.7 1.0
N A:ASP159 4.6 20.9 1.0
CA A:MET202 4.7 17.3 1.0
CG A:MET202 4.7 16.8 1.0
O A:VAL157 4.8 20.9 1.0
O A:LEU168 4.8 17.5 1.0
CA A:ASP159 4.9 20.9 1.0
CB A:ASN100 4.9 16.8 1.0
O A:HOH507 4.9 16.2 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 07:31:32 2024

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