AMINOPEPTIDASE P FROM E. COLI WITH THE INHIBITOR PRO-LEU
The structure was published by Wilce, M.C., Bond, C.S., Dixon, N.E., et al., Guss, J.M., Lilley, P.E., and Wilce, J.A., in 1998 in a paper entitled "Structure and mechanism of a proline-specific aminopeptidase from Escherichia coli." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.3 Å and deposited in 1997.
The experimental data on which the structure is based was not deposited.
The PDB entry contains the structure of AMINOPEPTIDASE P. This molecule has the UniProt identifier P15034 (AMPP_ECOLI). The sample contained 440 residues which is 100% of the natural sequence. Out of 440 residues 439 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 homotetramers.
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: