CRYSTALLOGRAPHIC ANALYSIS OF A PEPSTATIN ANALOGUE BINDING TO THE ASPARTYL PROTEINASE PENICILLOPEPSIN AT 1.8 ANGSTROMS RESOLUTION
The structure was published by James, M.N.G., Sielecki, A.R., and Moult, J., in 1983 in a paper entitled "Crystallographic Analysis of a Pepstatin Analogue Binding to the Aspartyl Proteinase Penicillopepsin at 1.8 Angstroms Resolution" (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 1.8 Å and deposited in 1991.
The experimental data on which the structure is based was not deposited.
This PDB entry contains a complex of 2 biomacromolecules, namely PENICILLOPEPSIN and INHIBITOR ISOVALERYL (IVA)-VAL-VAL-LYSTA-O-ET (LYSTA IS A LYSYL SIDE CHAIN ANALOGUE OF STATIN.
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 heterodimers.
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: