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Calcium in PDB 1kgu: Three Dimensional Structure Analysis of the R337A Variant of Human Pancreatic Alpha-Amylase

Enzymatic activity of Three Dimensional Structure Analysis of the R337A Variant of Human Pancreatic Alpha-Amylase

All present enzymatic activity of Three Dimensional Structure Analysis of the R337A Variant of Human Pancreatic Alpha-Amylase:
3.2.1.1;

Protein crystallography data

The structure of Three Dimensional Structure Analysis of the R337A Variant of Human Pancreatic Alpha-Amylase, PDB code: 1kgu was solved by S.Numao, R.Maurus, G.Sidhu, Y.Wang, C.M.Overall, G.D.Brayer, S.G.Withers, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 2.00
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 53.062, 74.984, 137.108, 90.00, 90.00, 90.00
R / Rfree (%) 19.3 / n/a

Calcium Binding Sites:

The binding sites of Calcium atom in the Three Dimensional Structure Analysis of the R337A Variant of Human Pancreatic Alpha-Amylase (pdb code 1kgu). 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 Three Dimensional Structure Analysis of the R337A Variant of Human Pancreatic Alpha-Amylase, PDB code: 1kgu:

Calcium binding site 1 out of 1 in 1kgu

Go back to Calcium Binding Sites List in 1kgu
Calcium binding site 1 out of 1 in the Three Dimensional Structure Analysis of the R337A Variant of Human Pancreatic Alpha-Amylase


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Three Dimensional Structure Analysis of the R337A Variant of Human Pancreatic Alpha-Amylase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca497

b:23.7
occ:1.00
 O A:HIS201 2.5 18.1 1.0
OD1 A:ASN100 2.5 17.8 1.0
O A:ARG158 2.5 19.3 1.0
OD2 A:ASP167 2.6 24.3 1.0
O A:HOH541 2.6 22.1 1.0
O A:HOH598 2.7 25.2 1.0
O A:HOH547 2.7 24.2 1.0
OD1 A:ASP167 2.7 22.1 1.0
CG A:ASP167 3.0 23.8 1.0
C A:ARG158 3.5 22.0 1.0
CG A:ASN100 3.6 18.7 1.0
C A:HIS201 3.6 16.9 1.0
ND2 A:ASN100 4.0 13.0 1.0
CA A:ARG158 4.1 20.1 1.0
CB A:HIS201 4.2 14.7 1.0
O A:ASN100 4.3 16.9 1.0
CA A:HIS201 4.5 17.3 1.0
CB A:ASP167 4.5 20.1 1.0
O A:HOH579 4.5 23.3 1.0
N A:MET202 4.5 17.3 1.0
ND2 A:ASN137 4.5 19.4 1.0
N A:ASP159 4.6 24.6 1.0
CA A:MET202 4.6 17.6 1.0
O A:VAL157 4.7 22.4 1.0
O A:CYS160 4.8 27.5 1.0
CG A:MET202 4.8 16.6 1.0
O A:LEU168 4.8 18.5 1.0
CB A:ASN100 4.9 14.1 1.0
CA A:ASP159 4.9 26.0 1.0
CB A:ARG158 5.0 20.6 1.0
O A:HOH549 5.0 19.5 1.0

Reference:

S.Numao, R.Maurus, G.Sidhu, Y.Wang, C.M.Overall, G.D.Brayer, S.G.Withers. Probing the Role of the Chloride Ion in the Mechanism of Human Pancreatic Alpha-Amylase. Biochemistry V. 41 215 2002.
ISSN: ISSN 0006-2960
PubMed: 11772019
DOI: 10.1021/BI0115636
Page generated: Mon Jul 7 16:29:04 2025

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