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Magnesium in PDB 7ujp: Cocrystal Structure of Human Camkii-Alpha (CAMK2A)Kinase Domain and GLUN2BEnzymatic activity of Cocrystal Structure of Human Camkii-Alpha (CAMK2A)Kinase Domain and GLUN2B
All present enzymatic activity of Cocrystal Structure of Human Camkii-Alpha (CAMK2A)Kinase Domain and GLUN2B:
2.7.11.17; Protein crystallography data
The structure of Cocrystal Structure of Human Camkii-Alpha (CAMK2A)Kinase Domain and GLUN2B, PDB code: 7ujp
was solved by
C.Ozden,
J.C.Foster,
M.M.Stratton,
S.C.Garman,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Cocrystal Structure of Human Camkii-Alpha (CAMK2A)Kinase Domain and GLUN2B
(pdb code 7ujp). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 3 binding sites of Magnesium where determined in the Cocrystal Structure of Human Camkii-Alpha (CAMK2A)Kinase Domain and GLUN2B, PDB code: 7ujp: Jump to Magnesium binding site number: 1; 2; 3; Magnesium binding site 1 out of 3 in 7ujpGo back to Magnesium Binding Sites List in 7ujp
Magnesium binding site 1 out
of 3 in the Cocrystal Structure of Human Camkii-Alpha (CAMK2A)Kinase Domain and GLUN2B
Mono view Stereo pair view
Magnesium binding site 2 out of 3 in 7ujpGo back to Magnesium Binding Sites List in 7ujp
Magnesium binding site 2 out
of 3 in the Cocrystal Structure of Human Camkii-Alpha (CAMK2A)Kinase Domain and GLUN2B
Mono view Stereo pair view
Magnesium binding site 3 out of 3 in 7ujpGo back to Magnesium Binding Sites List in 7ujp
Magnesium binding site 3 out
of 3 in the Cocrystal Structure of Human Camkii-Alpha (CAMK2A)Kinase Domain and GLUN2B
Mono view Stereo pair view
Reference:
C.Ozden,
R.Sloutsky,
T.Mitsugi,
N.Santos,
E.Agnello,
C.Gaubitz,
J.Foster,
E.Lapinskas,
E.A.Esposito,
T.Saneyoshi,
B.A.Kelch,
S.C.Garman,
Y.Hayashi,
M.M.Stratton.
Camkii Binds Both Substrates and Activators at the Active Site. Cell Rep V. 40 11064 2022.
Page generated: Thu Apr 6 23:51:36 2023
ISSN: ESSN 2211-1247 PubMed: 35830796 DOI: 10.1016/J.CELREP.2022.111064 |
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