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Atomistry » Magnesium » PDB 1zk3-207d » 1zy5 » |
Magnesium in PDB 1zy5: Crystal Structure of EIF2ALPHA Protein Kinase GCN2: R794G Hyperactivating Mutant Complexed with Amppnp.Enzymatic activity of Crystal Structure of EIF2ALPHA Protein Kinase GCN2: R794G Hyperactivating Mutant Complexed with Amppnp.
All present enzymatic activity of Crystal Structure of EIF2ALPHA Protein Kinase GCN2: R794G Hyperactivating Mutant Complexed with Amppnp.:
2.7.1.37; Protein crystallography data
The structure of Crystal Structure of EIF2ALPHA Protein Kinase GCN2: R794G Hyperactivating Mutant Complexed with Amppnp., PDB code: 1zy5
was solved by
A.K.Padyana,
H.Qiu,
A.Roll-Mecak,
A.G.Hinnebusch,
S.K.Burley,
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 EIF2ALPHA Protein Kinase GCN2: R794G Hyperactivating Mutant Complexed with Amppnp.
(pdb code 1zy5). 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 EIF2ALPHA Protein Kinase GCN2: R794G Hyperactivating Mutant Complexed with Amppnp., PDB code: 1zy5: Jump to Magnesium binding site number: 1; 2; Magnesium binding site 1 out of 2 in 1zy5Go back to Magnesium Binding Sites List in 1zy5
Magnesium binding site 1 out
of 2 in the Crystal Structure of EIF2ALPHA Protein Kinase GCN2: R794G Hyperactivating Mutant Complexed with Amppnp.
Mono view Stereo pair view
Magnesium binding site 2 out of 2 in 1zy5Go back to Magnesium Binding Sites List in 1zy5
Magnesium binding site 2 out
of 2 in the Crystal Structure of EIF2ALPHA Protein Kinase GCN2: R794G Hyperactivating Mutant Complexed with Amppnp.
Mono view Stereo pair view
Reference:
A.K.Padyana,
H.Qiu,
A.Roll-Mecak,
A.G.Hinnebusch,
S.K.Burley.
Structural Basis For Autoinhibition and Mutational Activation of Eukaryotic Initiation Factor 2{Alpha} Protein Kinase GCN2 J.Biol.Chem. V. 280 29289 2005.
Page generated: Tue Aug 13 20:16:12 2024
ISSN: ISSN 0021-9258 PubMed: 15964839 DOI: 10.1074/JBC.M504096200 |
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