The aminopeptidase from Aeromonas proteolytica (AAP) is a bridged bimetallic enzyme that removes the N-terminal amino acid from a peptide chain. To fully understand the metal roles in the reaction pathway of AAP we have solved the 1.20 A resolution crystal structure of native AAP (PDB ID = 1LOK). The high-quality electron density maps showed a single Tris molecule chelated to the active site Zn(2+), alternate side chain conformations for some side chains, a sodium ion that mediates a crystal contact, a surface thiocyanate ion, and several potential hydrogen atoms. In addition, the high precision of the atomic positions has led to insight into the protonation states of some of the active site amino acid side chains.
This research output has an Altmetric Attention Score of 3. This is our high-level measure of the quality and quantity of online attention that it has received. This Attention Score, as well as the ranking and number of research outputs shown below, was calculated when the research output was last mentioned on 09 February 2026.
All research outputs
#9,515,738
of 27,782,313 outputs
Outputs from Structure
#1,984
of 3,957 outputs
Outputs of similar age
#19,882
of 54,224 outputs
Outputs of similar age from Structure
#7
of 22 outputs
Altmetric has tracked 27,782,313 research outputs across all sources so far. This one is in the 42nd percentile – i.e., 42% of other outputs scored the same or lower than it.
So far Altmetric has tracked 3,957 research outputs from this source. They typically receive more attention than average, with a mean Attention Score of 7.5. This one is in the 29th percentile – i.e., 29% of its peers scored the same or lower than it.
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We're also able to compare this research output to 22 others from the same source and published within six weeks on either side of this one. This one is in the 9th percentile – i.e., 9% of its contemporaries scored the same or lower than it.
