1amp Summary

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CRYSTAL STRUCTURE OF AEROMONAS PROTEOLYTICA AMINOPEPTIDASE: A PROTOTYPICAL MEMBER OF THE CO-CATALYTIC ZINC ENZYME FAMILY

The structure was published by Chevrier, B., Schalk, C., D'Orchymont, H., Rondeau, J.M., Moras, D., and Tarnus, C., in 1994 in a paper entitled "Crystal structure of Aeromonas proteolytica aminopeptidase: a prototypical member of the co-catalytic zinc enzyme family." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.8 Å and deposited in 1994.

The experimental data on which the structure is based was also deposited.

The PDB entry contains the structure of AMINOPEPTIDASE. This molecule has the UniProt identifier Q01693 (AMPX_VIBPR)search. The sample contained 291 residues which is < 90% of the natural sequence. Out of 291 residues 290 were observed and are deposited in the PDB.

It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.

The molecule most likely forms homodimers.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):


Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A AMINOPEPTIDASE Q01693 (107-397) (AMPX_VIBPR)search Vibrio proteolyticussearch < 90% 291 100%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
Q01693 (107 - 397) AMINOPEPTIDASE Vibrio proteolyticus

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A Bacterial dinuclear zinc exopeptidasessearch Zn peptidasessearch Peptidase family M28search

Chain ID Molecular function (GO) Biological process (GO)
A (Q01693) peptidase activitysearch proteolysissearch

Chain InterPro annotation
A Peptidase M28search Peptidase M28E, aminopeptidase AP1search