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Atomistry » Magnesium » PDB 3o1n-3oha » 3o7l | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Magnesium » PDB 3o1n-3oha » 3o7l » |
Magnesium in PDB 3o7l: Crystal Structure of Phospholamban (1-19):Pka C-Subunit:Amp-Pnp:MG2+ ComplexEnzymatic activity of Crystal Structure of Phospholamban (1-19):Pka C-Subunit:Amp-Pnp:MG2+ Complex
All present enzymatic activity of Crystal Structure of Phospholamban (1-19):Pka C-Subunit:Amp-Pnp:MG2+ Complex:
2.7.11.11; Protein crystallography data
The structure of Crystal Structure of Phospholamban (1-19):Pka C-Subunit:Amp-Pnp:MG2+ Complex, PDB code: 3o7l
was solved by
C.Y.Cheng,
S.S.Taylor,
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 Crystal Structure of Phospholamban (1-19):Pka C-Subunit:Amp-Pnp:MG2+ Complex
(pdb code 3o7l). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of Phospholamban (1-19):Pka C-Subunit:Amp-Pnp:MG2+ Complex, PDB code: 3o7l: Jump to Magnesium binding site number: 1; 2; Magnesium binding site 1 out of 2 in 3o7lGo back to Magnesium Binding Sites List in 3o7l
Magnesium binding site 1 out
of 2 in the Crystal Structure of Phospholamban (1-19):Pka C-Subunit:Amp-Pnp:MG2+ Complex
Mono view Stereo pair view
Magnesium binding site 2 out of 2 in 3o7lGo back to Magnesium Binding Sites List in 3o7l
Magnesium binding site 2 out
of 2 in the Crystal Structure of Phospholamban (1-19):Pka C-Subunit:Amp-Pnp:MG2+ Complex
Mono view Stereo pair view
Reference:
L.R.Masterson,
C.Cheng,
T.Yu,
M.Tonelli,
A.Kornev,
S.S.Taylor,
G.Veglia.
Dynamics Connect Substrate Recognition to Catalysis in Protein Kinase A. Nat.Chem.Biol. V. 6 821 2010.
Page generated: Thu Aug 15 08:12:48 2024
ISSN: ISSN 1552-4450 PubMed: 20890288 DOI: 10.1038/NCHEMBIO.452 |
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