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Chlorine in PDB 6b2e: Structure of Full Length Human Ampk (A2B2G1) in Complex with A Small Molecule Activator SC4.Enzymatic activity of Structure of Full Length Human Ampk (A2B2G1) in Complex with A Small Molecule Activator SC4.
All present enzymatic activity of Structure of Full Length Human Ampk (A2B2G1) in Complex with A Small Molecule Activator SC4.:
2.7.11.1; 2.7.11.27; 2.7.11.31; Protein crystallography data
The structure of Structure of Full Length Human Ampk (A2B2G1) in Complex with A Small Molecule Activator SC4., PDB code: 6b2e
was solved by
K.R.W.Ngoei,
C.G.Langendorf,
N.X.Y.Ling,
A.Hoque,
S.Johnson,
M.C.Camerino,
S.R.Walker,
Y.E.Bozikis,
T.A.Dite,
A.J.Ovens,
W.J.Smiles,
R.Jacobs,
H.Huang,
M.W.Parker,
J.W.Scott,
M.H.Rider,
B.E.Kemp,
R.C.Foitzik,
J.B.Baell,
J.S.Oakhill,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Structure of Full Length Human Ampk (A2B2G1) in Complex with A Small Molecule Activator SC4.
(pdb code 6b2e). 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 Structure of Full Length Human Ampk (A2B2G1) in Complex with A Small Molecule Activator SC4., PDB code: 6b2e: Chlorine binding site 1 out of 1 in 6b2eGo back to Chlorine Binding Sites List in 6b2e
Chlorine binding site 1 out
of 1 in the Structure of Full Length Human Ampk (A2B2G1) in Complex with A Small Molecule Activator SC4.
Mono view Stereo pair view
Reference:
K.R.W.Ngoei,
C.G.Langendorf,
N.X.Y.Ling,
A.Hoque,
S.Varghese,
M.A.Camerino,
S.R.Walker,
Y.E.Bozikis,
T.A.Dite,
A.J.Ovens,
W.J.Smiles,
R.Jacobs,
H.Huang,
M.W.Parker,
J.W.Scott,
M.H.Rider,
R.C.Foitzik,
B.E.Kemp,
J.B.Baell,
J.S.Oakhill.
Structural Determinants For Small-Molecule Activation of Skeletal Muscle Ampk Alpha 2 Beta 2 Gamma 1 By the Glucose Importagog SC4. Cell Chem Biol V. 25 728 2018.
Page generated: Sat Dec 12 12:45:09 2020
ISSN: ESSN 2451-9448 PubMed: 29657085 DOI: 10.1016/J.CHEMBIOL.2018.03.008 |
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