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Calcium in PDB 3ij8: Directed 'in Situ' Elongation As A Strategy to Characterize the Covalent Glycosyl-Enzyme Catalytic Intermediate of Human Pancreatic A-Amylase

Enzymatic activity of Directed 'in Situ' Elongation As A Strategy to Characterize the Covalent Glycosyl-Enzyme Catalytic Intermediate of Human Pancreatic A-Amylase

All present enzymatic activity of Directed 'in Situ' Elongation As A Strategy to Characterize the Covalent Glycosyl-Enzyme Catalytic Intermediate of Human Pancreatic A-Amylase:
3.2.1.1;

Protein crystallography data

The structure of Directed 'in Situ' Elongation As A Strategy to Characterize the Covalent Glycosyl-Enzyme Catalytic Intermediate of Human Pancreatic A-Amylase, PDB code: 3ij8 was solved by C.Li, R.Zhang, 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) 29.33 / 1.43
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 52.000, 68.470, 129.860, 90.00, 90.00, 90.00
R / Rfree (%) 19.7 / 21.3

Other elements in 3ij8:

The structure of Directed 'in Situ' Elongation As A Strategy to Characterize the Covalent Glycosyl-Enzyme Catalytic Intermediate of Human Pancreatic A-Amylase also contains other interesting chemical elements:

Fluorine (F) 7 atoms
Chlorine (Cl) 1 atom

Calcium Binding Sites:

The binding sites of Calcium atom in the Directed 'in Situ' Elongation As A Strategy to Characterize the Covalent Glycosyl-Enzyme Catalytic Intermediate of Human Pancreatic A-Amylase (pdb code 3ij8). 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 Directed 'in Situ' Elongation As A Strategy to Characterize the Covalent Glycosyl-Enzyme Catalytic Intermediate of Human Pancreatic A-Amylase, PDB code: 3ij8:

Calcium binding site 1 out of 1 in 3ij8

Go back to Calcium Binding Sites List in 3ij8
Calcium binding site 1 out of 1 in the Directed 'in Situ' Elongation As A Strategy to Characterize the Covalent Glycosyl-Enzyme Catalytic Intermediate of Human Pancreatic A-Amylase


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Directed 'in Situ' Elongation As A Strategy to Characterize the Covalent Glycosyl-Enzyme Catalytic Intermediate of Human Pancreatic A-Amylase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca497

b:12.5
occ:1.00
 OD1 A:ASN100 2.4 13.4 1.0
O A:ARG158 2.4 14.6 1.0
O A:HIS201 2.4 13.2 1.0
OD2 A:ASP167 2.5 14.1 1.0
OD1 A:ASP167 2.5 13.2 1.0
O A:HOH730 2.6 16.0 1.0
CG A:ASP167 2.8 12.5 1.0
C A:ARG158 3.4 14.5 1.0
CG A:ASN100 3.5 12.1 1.0
C A:HIS201 3.6 13.0 1.0
ND2 A:ASN100 4.0 13.6 1.0
CA A:ARG158 4.0 14.8 1.0
CB A:HIS201 4.2 13.2 1.0
CB A:ASP167 4.3 12.8 1.0
O A:ASN100 4.4 13.3 1.0
CA A:HIS201 4.4 13.7 1.0
N A:ASP159 4.5 14.2 1.0
ND2 A:ASN137 4.5 16.1 1.0
O A:HOH539 4.5 16.6 1.0
O A:CYS160 4.6 14.8 1.0
N A:MET202 4.6 12.6 1.0
CA A:MET202 4.7 13.5 1.0
O A:VAL157 4.7 14.5 1.0
CB A:ASN100 4.8 13.0 1.0
CA A:ASP159 4.8 15.0 1.0
O A:LEU168 4.8 13.8 1.0
CG A:MET202 4.8 13.2 1.0
O A:HOH727 4.9 13.3 1.0
CB A:ARG158 4.9 15.1 1.0

Reference:

R.Zhang, C.Li, L.K.Williams, B.P.Rempel, G.D.Brayer, S.G.Withers. Directed "in Situ" Inhibitor Elongation As A Strategy to Structurally Characterize the Covalent Glycosyl-Enzyme Intermediate of Human Pancreatic Alpha-Amylase Biochemistry V. 48 10752 2009.
ISSN: ISSN 0006-2960
PubMed: 19803533
DOI: 10.1021/BI901400P
Page generated: Sat Jul 13 11:35:32 2024

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