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Atomistry » Chlorine » PDB 1hba-1i3k » 1hny | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Chlorine » PDB 1hba-1i3k » 1hny » |
Chlorine in PDB 1hny: The Structure of Human Pancreatic Alpha-Amylase at 1.8 Angstroms Resolution and Comparisons with Related EnzymesEnzymatic activity of The Structure of Human Pancreatic Alpha-Amylase at 1.8 Angstroms Resolution and Comparisons with Related Enzymes
All present enzymatic activity of The Structure of Human Pancreatic Alpha-Amylase at 1.8 Angstroms Resolution and Comparisons with Related Enzymes:
3.2.1.1; Protein crystallography data
The structure of The Structure of Human Pancreatic Alpha-Amylase at 1.8 Angstroms Resolution and Comparisons with Related Enzymes, PDB code: 1hny
was solved by
Y.Luo,
G.D.Brayer,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 1hny:
The structure of The Structure of Human Pancreatic Alpha-Amylase at 1.8 Angstroms Resolution and Comparisons with Related Enzymes also contains other interesting chemical elements:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the The Structure of Human Pancreatic Alpha-Amylase at 1.8 Angstroms Resolution and Comparisons with Related Enzymes
(pdb code 1hny). This binding sites where shown within
5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the The Structure of Human Pancreatic Alpha-Amylase at 1.8 Angstroms Resolution and Comparisons with Related Enzymes, PDB code: 1hny: Chlorine binding site 1 out of 1 in 1hnyGo back to![]() ![]()
Chlorine binding site 1 out
of 1 in the The Structure of Human Pancreatic Alpha-Amylase at 1.8 Angstroms Resolution and Comparisons with Related Enzymes
![]() Mono view ![]() Stereo pair view
Reference:
G.D.Brayer,
Y.Luo,
S.G.Withers.
The Structure of Human Pancreatic Alpha-Amylase at 1.8 A Resolution and Comparisons with Related Enzymes. Protein Sci. V. 4 1730 1995.
Page generated: Thu Jul 10 17:15:34 2025
ISSN: ISSN 0961-8368 PubMed: 8528071 |
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