5cnx

Crystal structure of Xaa-Pro aminopeptidase from Escherichia coli K12Crystal structure of Xaa-Pro aminopeptidase from Escherichia coli K12

Structural highlights

5cnx is a 3 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[YPDF_ECOLI] Hydrolyzes the N-terminal methionine when the next amino acid is alanine, proline or serine. The substrate preference for methionyl aminopeptidase activity is Pro > Ala > Ser. Also able to hydrolyze the Xaa-Pro peptide bond when the first amino acid is alanine, asparagine or methionine.^[1]

References

↑ Zheng Y, Roberts RJ, Kasif S, Guan C. Characterization of two new aminopeptidases in Escherichia coli. J Bacteriol. 2005 Jun;187(11):3671-7. PMID:15901689 doi:http://dx.doi.org/187/11/3671

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OCA

[1] Zheng Y, Roberts RJ, Kasif S, Guan C. Characterization of two new aminopeptidases in Escherichia coli. J Bacteriol. 2005 Jun;187(11):3671-7. PMID:15901689 doi:http://dx.doi.org/187/11/3671

[1]

5cnx

Crystal structure of Xaa-Pro aminopeptidase from Escherichia coli K12Crystal structure of Xaa-Pro aminopeptidase from Escherichia coli K12

Structural highlights

Function

References

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5cnx

Crystal structure of Xaa-Pro aminopeptidase from Escherichia coli K12Crystal structure of Xaa-Pro aminopeptidase from Escherichia coli K12

Structural highlights

Function

References

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