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Atomistry » Manganese » PDB 2pal-2qgi » 2phk » |
Manganese in PDB 2phk: The Crystal Structure of A Phosphorylase Kinase Peptide Substrate Complex: Kinase Substrate RecognitionEnzymatic activity of The Crystal Structure of A Phosphorylase Kinase Peptide Substrate Complex: Kinase Substrate Recognition
All present enzymatic activity of The Crystal Structure of A Phosphorylase Kinase Peptide Substrate Complex: Kinase Substrate Recognition:
2.7.1.38; Protein crystallography data
The structure of The Crystal Structure of A Phosphorylase Kinase Peptide Substrate Complex: Kinase Substrate Recognition, PDB code: 2phk
was solved by
E.D.Lowe,
M.E.M.Noble,
V.T.Skamnaki,
N.G.Oikonomakos,
D.J.Owen,
L.N.Johnson,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Manganese Binding Sites:
The binding sites of Manganese atom in the The Crystal Structure of A Phosphorylase Kinase Peptide Substrate Complex: Kinase Substrate Recognition
(pdb code 2phk). This binding sites where shown within
5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the The Crystal Structure of A Phosphorylase Kinase Peptide Substrate Complex: Kinase Substrate Recognition, PDB code: 2phk: Jump to Manganese binding site number: 1; 2; Manganese binding site 1 out of 2 in 2phkGo back to Manganese Binding Sites List in 2phk
Manganese binding site 1 out
of 2 in the The Crystal Structure of A Phosphorylase Kinase Peptide Substrate Complex: Kinase Substrate Recognition
Mono view Stereo pair view
Manganese binding site 2 out of 2 in 2phkGo back to Manganese Binding Sites List in 2phk
Manganese binding site 2 out
of 2 in the The Crystal Structure of A Phosphorylase Kinase Peptide Substrate Complex: Kinase Substrate Recognition
Mono view Stereo pair view
Reference:
E.D.Lowe,
M.E.Noble,
V.T.Skamnaki,
N.G.Oikonomakos,
D.J.Owen,
L.N.Johnson.
The Crystal Structure of A Phosphorylase Kinase Peptide Substrate Complex: Kinase Substrate Recognition. Embo J. V. 16 6646 1997.
Page generated: Sat Oct 5 14:53:54 2024
ISSN: ISSN 0261-4189 PubMed: 9362479 DOI: 10.1093/EMBOJ/16.22.6646 |
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