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Phosphorus in PDB 1akc: Structural Basis For the Catalytic Activity of Aspartate Aminotransferase K258H Lacking Its Pyridoxal-5'-Phosphate-Binding Lysine ResidueEnzymatic activity of Structural Basis For the Catalytic Activity of Aspartate Aminotransferase K258H Lacking Its Pyridoxal-5'-Phosphate-Binding Lysine Residue
All present enzymatic activity of Structural Basis For the Catalytic Activity of Aspartate Aminotransferase K258H Lacking Its Pyridoxal-5'-Phosphate-Binding Lysine Residue:
2.6.1.1; Protein crystallography data
The structure of Structural Basis For the Catalytic Activity of Aspartate Aminotransferase K258H Lacking Its Pyridoxal-5'-Phosphate-Binding Lysine Residue, PDB code: 1akc
was solved by
V.N.Malashkevich,
J.N.Jansonius,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Phosphorus Binding Sites:
The binding sites of Phosphorus atom in the Structural Basis For the Catalytic Activity of Aspartate Aminotransferase K258H Lacking Its Pyridoxal-5'-Phosphate-Binding Lysine Residue
(pdb code 1akc). This binding sites where shown within
5.0 Angstroms radius around Phosphorus atom.
In total only one binding site of Phosphorus was determined in the Structural Basis For the Catalytic Activity of Aspartate Aminotransferase K258H Lacking Its Pyridoxal-5'-Phosphate-Binding Lysine Residue, PDB code: 1akc: Phosphorus binding site 1 out of 1 in 1akcGo back to Phosphorus Binding Sites List in 1akc
Phosphorus binding site 1 out
of 1 in the Structural Basis For the Catalytic Activity of Aspartate Aminotransferase K258H Lacking Its Pyridoxal-5'-Phosphate-Binding Lysine Residue
Mono view Stereo pair view
Reference:
V.N.Malashkevich,
J.Jager,
M.Ziak,
U.Sauder,
H.Gehring,
P.Christen,
J.N.Jansonius.
Structural Basis For the Catalytic Activity of Aspartate Aminotransferase K258H Lacking the Pyridoxal 5'-Phosphate-Binding Lysine Residue. Biochemistry V. 34 405 1995.
Page generated: Fri Sep 25 13:04:25 2020
ISSN: ISSN 0006-2960 PubMed: 7819232 DOI: 10.1021/BI00002A004 |
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