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PDBe Entry: 1jaw 
AMINOPEPTIDASE P FROM E. COLI LOW PH FORM
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PROLINE PEPTIDASE
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X-RAY DIFFRACTION
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Resolution: 2.7 Å, R-factor: 18.2%, Free R-factor: 22.7%, Spacegroup: I 41 2 2
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06/04/1999, deposition: 22/12/1997, last revision: 24/02/2009
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Wilce, M.C.J.; Bond, C.S.; Lilley, P.E.; Dixon, N.E.; Freeman, H.C.; Guss, J.M.
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Structure and mechanism of a proline-specific aminopeptidase from Escherichia coli.
PROC.NATL.ACAD.SCI.USA vol:95, pag:3472-3477 (1998) [PubMed ID 9520390 ]
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PROLINE PEPTIDASE, HYDROLASE, AMINOPEPTIDASE
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3.4.11.9 ExPASy BRENDA (A)
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Escherichia coli 562(A)
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Xaa-Pro aminopeptidase (EC 3.4.11.9) (X-Pro aminopeptidase) (Aminopeptidase P II) (APP-II) (Aminoacylproline aminopeptidase) P15034 (A)
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A
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| A |
AMINOPEPTIDASE P |
Protein |
P15034 (AMPP_ECOLI)
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440 |
100% |
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| A |
MANGANESE (II) ION |
MN
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| A |
ACETATE ION |
ACT
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