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Atomistry » Chlorine » PDB 1pu6-1qhu » 1q4n | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Chlorine » PDB 1pu6-1qhu » 1q4n » |
Chlorine in PDB 1q4n: Structural Studies of PHE256TRP of Human Salivary Alpha-Amylase: Implications For the Role of A Conserved Water Molecule and Its Associated Chain in Enzyme ActivityEnzymatic activity of Structural Studies of PHE256TRP of Human Salivary Alpha-Amylase: Implications For the Role of A Conserved Water Molecule and Its Associated Chain in Enzyme Activity
All present enzymatic activity of Structural Studies of PHE256TRP of Human Salivary Alpha-Amylase: Implications For the Role of A Conserved Water Molecule and Its Associated Chain in Enzyme Activity:
3.2.1.1; Protein crystallography data
The structure of Structural Studies of PHE256TRP of Human Salivary Alpha-Amylase: Implications For the Role of A Conserved Water Molecule and Its Associated Chain in Enzyme Activity, PDB code: 1q4n
was solved by
N.Ramasubbu,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 1q4n:
The structure of Structural Studies of PHE256TRP of Human Salivary Alpha-Amylase: Implications For the Role of A Conserved Water Molecule and Its Associated Chain in Enzyme Activity also contains other interesting chemical elements:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Structural Studies of PHE256TRP of Human Salivary Alpha-Amylase: Implications For the Role of A Conserved Water Molecule and Its Associated Chain in Enzyme Activity
(pdb code 1q4n). 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 Structural Studies of PHE256TRP of Human Salivary Alpha-Amylase: Implications For the Role of A Conserved Water Molecule and Its Associated Chain in Enzyme Activity, PDB code: 1q4n: Chlorine binding site 1 out of 1 in 1q4nGo back to![]() ![]()
Chlorine binding site 1 out
of 1 in the Structural Studies of PHE256TRP of Human Salivary Alpha-Amylase: Implications For the Role of A Conserved Water Molecule and Its Associated Chain in Enzyme Activity
![]() Mono view ![]() Stereo pair view
Reference:
N.Ramasubbu,
K.Sundar,
C.Ragunath,
M.M.Rafi.
Structural Studies of A PHE256TRP Mutant of Human Salivary Alpha-Amylase: Implications For the Role of A Conserved Water Molecule in Enzyme Activity Arch.Biochem.Biophys. V. 421 115 2004.
Page generated: Sat Jul 20 01:22:53 2024
ISSN: ISSN 0003-9861 PubMed: 14678792 DOI: 10.1016/J.ABB.2003.10.007 |
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