1aic | pdb_00001aic

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File:1aic.png

Template:STRUCTURE 1aic

STRUCTURAL BASIS FOR THE CATALYTIC ACTIVITY OF ASPARTATE AMINOTRANSFERASE K258H LACKING THE PYRIDOXAL-5'-PHSOPHATE BINDING LYSINE RESIDUE

Template:ABSTRACT PUBMED 7819232

About this Structure

1AIC is a 2 chains structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Malashkevich VN, Jager J, Ziak M, Sauder U, Gehring H, Christen P, Jansonius JN. Structural basis for the catalytic activity of aspartate aminotransferase K258H lacking the pyridoxal 5'-phosphate-binding lysine residue. Biochemistry. 1995 Jan 17;34(2):405-14. PMID:7819232

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OCA

[1] Malashkevich VN, Jager J, Ziak M, Sauder U, Gehring H, Christen P, Jansonius JN. Structural basis for the catalytic activity of aspartate aminotransferase K258H lacking the pyridoxal 5'-phosphate-binding lysine residue. Biochemistry. 1995 Jan 17;34(2):405-14. PMID:7819232

1aic | pdb_00001aic

STRUCTURAL BASIS FOR THE CATALYTIC ACTIVITY OF ASPARTATE AMINOTRANSFERASE K258H LACKING THE PYRIDOXAL-5'-PHSOPHATE BINDING LYSINE RESIDUE

About this Structure

Reference

Proteopedia Page Contributors and Editors (what is this?)

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