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Fluorine in PDB 3ij7: 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;
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: 3ij7
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) | 28.43 / 2.00 |
| Space group | P 21 21 21 |
| Cell size a, b, c (Å), α, β, γ (°) | 52.140, 67.820, 129.920, 90.00, 90.00, 90.00 |
| R / Rfree (%) | 19.3 / 22.9 |
Other elements in 3ij7:
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:
| Chlorine | (Cl) | 1 atom |
| Calcium | (Ca) | 1 atom |
Fluorine Binding Sites:
The binding sites of Fluorine 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 3ij7). This binding sites where shown within
5.0 Angstroms radius around Fluorine atom.
In total 2 binding sites of Fluorine where 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: 3ij7:
Jump to Fluorine binding site number: 1; 2;
In total 2 binding sites of Fluorine where 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: 3ij7:
Jump to Fluorine binding site number: 1; 2;
Fluorine binding site 1 out of 2 in 3ij7
Go back to
Fluorine Binding Sites List in 3ij7
Fluorine binding site 1 out
of 2 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
Mono view
Stereo pair view
A full contact list of Fluorine with other atoms in the F 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:
|
Fluorine binding site 2 out of 2 in 3ij7
Go back to
Fluorine Binding Sites List in 3ij7
Fluorine binding site 2 out
of 2 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
Mono view
Stereo pair view
A full contact list of Fluorine with other atoms in the F binding
site number 2 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:
|
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: Wed Jul 31 19:31:53 2024
ISSN: ISSN 0006-2960
PubMed: 19803533
DOI: 10.1021/BI901400P
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