The 1.20 Angstrom Resolution Crystal Structure of the Aminopeptidase from Aeromonas proteolytica Complexed with Tris: A Tale of Buffer Inhibition
The structure was published by Desmarais, W.T., Bienvenue, D.L., Bzymek, K.P., Holz, R.C., Petsko, G.A., and Ringe, D., in 2002 in a paper entitled "The 1.20 Angstrom Resolution Crystal Structure of the Aminopeptidase from Aeromonas proteolytica Complexed with Tris A tale of Buffer Inhibition" (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 1.2 Å and deposited in 2002.
The experimental data on which the structure is based was not deposited.
The PDB entry contains the structure of Bacterial leucyl aminopeptidase. This molecule has the UniProt identifier Q01693 (AMPX_VIBPR). The sample contained 291 residues which is < 90% of the natural sequence. Out of 291 residues 291 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 is most likely monomeric.
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):
This entry contains 1 unique UniProt protein: