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Atomistry » Calcium » PDB 5hsa-5i6w » 5hxm | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Calcium » PDB 5hsa-5i6w » 5hxm » |
Calcium in PDB 5hxm: Cycloalternan-Forming Enzyme From Listeria Monocytogenes in Complex with PanoseEnzymatic activity of Cycloalternan-Forming Enzyme From Listeria Monocytogenes in Complex with Panose
All present enzymatic activity of Cycloalternan-Forming Enzyme From Listeria Monocytogenes in Complex with Panose:
3.2.1.177; Protein crystallography data
The structure of Cycloalternan-Forming Enzyme From Listeria Monocytogenes in Complex with Panose, PDB code: 5hxm
was solved by
A.S.Halavaty,
S.H.Light,
G.Minasov,
J.Winsor,
S.Grimshaw,
L.Shuvalova,
S.Peterson,
W.F.Anderson,
Center For Structural Genomics Of Infectiousdiseases (Csgid),
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 5hxm:
The structure of Cycloalternan-Forming Enzyme From Listeria Monocytogenes in Complex with Panose also contains other interesting chemical elements:
Calcium Binding Sites:
The binding sites of Calcium atom in the Cycloalternan-Forming Enzyme From Listeria Monocytogenes in Complex with Panose
(pdb code 5hxm). 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 Cycloalternan-Forming Enzyme From Listeria Monocytogenes in Complex with Panose, PDB code: 5hxm: Calcium binding site 1 out of 1 in 5hxmGo back to Calcium Binding Sites List in 5hxm
Calcium binding site 1 out
of 1 in the Cycloalternan-Forming Enzyme From Listeria Monocytogenes in Complex with Panose
Mono view Stereo pair view
Reference:
S.H.Light,
L.A.Cahoon,
K.V.Mahasenan,
M.Lee,
B.Boggess,
A.S.Halavaty,
S.Mobashery,
N.E.Freitag,
W.F.Anderson.
Transferase Versus Hydrolase: the Role of Conformational Flexibility in Reaction Specificity. Structure V. 25 295 2017.
Page generated: Sat Dec 12 05:29:28 2020
ISSN: ISSN 1878-4186 PubMed: 28089449 DOI: 10.1016/J.STR.2016.12.007 |
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