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Atomistry » Calcium » PDB 3ij7-3isv » 3ij7 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Calcium » PDB 3ij7-3isv » 3ij7 » |
Calcium in PDB 3ij7: Directed 'in Situ' Elongation As A Strategy to Characterize the Covalent Glycosyl-Enzyme Catalytic Intermediate of Human Pancreatic A-AmylaseEnzymatic 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: 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:
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:
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 3ij7). 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: 3ij7: Calcium binding site 1 out of 1 in 3ij7Go back to![]() ![]()
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
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.
Page generated: Sat Jul 13 11:35:32 2024
ISSN: ISSN 0006-2960 PubMed: 19803533 DOI: 10.1021/BI901400P |
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