1apt Summary

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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):


Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
E PENICILLOPEPSIN P00798 (1-323) (PENP_PENJA)search Penicillium janthinellumsearch 100% 323 100%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P00798 (1 - 323) PENICILLOPEPSIN Penicillium janthinellum

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
E (P00798) Pepsin-likesearch Acid Proteasessearch PF00026: Eukaryotic aspartyl proteasesearch

Chain ID Molecular function (GO) Biological process (GO)
E (P00798) aspartic-type endopeptidase activitysearch peptidase activitysearch hydrolase activitysearch proteolysissearch

Chain InterPro annotation
E Aspartic peptidasesearch Aspartic peptidase, active sitesearch Aspartic peptidase domainsearch