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Atomistry » Calcium » PDB 1mts-1n7d » 1mwo | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Calcium » PDB 1mts-1n7d » 1mwo » |
Calcium in PDB 1mwo: Crystal Structure Analysis of the Hyperthermostable Pyrocoocus Woesei Alpha-AmylaseEnzymatic activity of Crystal Structure Analysis of the Hyperthermostable Pyrocoocus Woesei Alpha-Amylase
All present enzymatic activity of Crystal Structure Analysis of the Hyperthermostable Pyrocoocus Woesei Alpha-Amylase:
3.2.1.1; Protein crystallography data
The structure of Crystal Structure Analysis of the Hyperthermostable Pyrocoocus Woesei Alpha-Amylase, PDB code: 1mwo
was solved by
A.Linden,
O.Mayans,
W.Meyer-Klaucke,
G.Antranikian,
M.Wilmanns,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 1mwo:
The structure of Crystal Structure Analysis of the Hyperthermostable Pyrocoocus Woesei Alpha-Amylase also contains other interesting chemical elements:
Calcium Binding Sites:
The binding sites of Calcium atom in the Crystal Structure Analysis of the Hyperthermostable Pyrocoocus Woesei Alpha-Amylase
(pdb code 1mwo). 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 Crystal Structure Analysis of the Hyperthermostable Pyrocoocus Woesei Alpha-Amylase, PDB code: 1mwo: Calcium binding site 1 out of 1 in 1mwoGo back to Calcium Binding Sites List in 1mwo
Calcium binding site 1 out
of 1 in the Crystal Structure Analysis of the Hyperthermostable Pyrocoocus Woesei Alpha-Amylase
Mono view Stereo pair view
Reference:
A.Linden,
O.Mayans,
W.Meyer-Klaucke,
G.Antranikian,
M.Wilmanns.
Differential Regulation of A Hyperthermophilic Alpha-Amylase with A Novel (Ca,Zn) Two-Metal Center By Zinc J.Biol.Chem. V. 278 9875 2003.
Page generated: Sat Dec 12 03:07:38 2020
ISSN: ISSN 0021-9258 PubMed: 12482867 DOI: 10.1074/JBC.M211339200 |
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