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Atomistry » Calcium » PDB 1qls-1ra1 » 1qpk | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Calcium » PDB 1qls-1ra1 » 1qpk » |
Calcium in PDB 1qpk: Mutant (D193G) Maltotetraose-Forming Exo-Amylase in Complex with MaltotetraoseProtein crystallography data
The structure of Mutant (D193G) Maltotetraose-Forming Exo-Amylase in Complex with Maltotetraose, PDB code: 1qpk
was solved by
Y.Yoshioka,
K.Hasegawa,
Y.Matsuura,
Y.Katsube,
M.Kubota,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Calcium Binding Sites:
The binding sites of Calcium atom in the Mutant (D193G) Maltotetraose-Forming Exo-Amylase in Complex with Maltotetraose
(pdb code 1qpk). This binding sites where shown within
5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Mutant (D193G) Maltotetraose-Forming Exo-Amylase in Complex with Maltotetraose, PDB code: 1qpk: Jump to Calcium binding site number: 1; 2; Calcium binding site 1 out of 2 in 1qpkGo back to![]() ![]()
Calcium binding site 1 out
of 2 in the Mutant (D193G) Maltotetraose-Forming Exo-Amylase in Complex with Maltotetraose
![]() Mono view ![]() Stereo pair view
Calcium binding site 2 out of 2 in 1qpkGo back to![]() ![]()
Calcium binding site 2 out
of 2 in the Mutant (D193G) Maltotetraose-Forming Exo-Amylase in Complex with Maltotetraose
![]() Mono view ![]() Stereo pair view
Reference:
K.Hasegawa,
M.Kubota,
Y.Matsuura.
Roles of Catalytic Residues in Alpha-Amylases As Evidenced By the Structures of the Product-Complexed Mutants of A Maltotetraose-Forming Amylase. Protein Eng. V. 12 819 1999.
Page generated: Thu Jul 11 21:57:37 2024
ISSN: ISSN 0269-2139 PubMed: 10556241 DOI: 10.1093/PROTEIN/12.10.819 |
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