1gec Summary

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GLYCYL ENDOPEPTIDASE-COMPLEX WITH BENZYLOXYCARBONYL-LEUCINE-VALINE-GLYCINE-METHYLENE COVALENTLY BOUND TO CYSTEINE 25

The structure was published by O'Hara, B.P., Hemmings, A.M., Buttle, D.J., and Pearl, L.H., in 1995 in a paper entitled "Crystal structure of glycyl endopeptidase from Carica papaya: a cysteine endopeptidase of unusual substrate specificity." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.1 Å and deposited in 1995.

The experimental data on which the structure is based was not deposited.

This PDB entry contains a complex of 2 biomacromolecules, namely GLYCYL ENDOPEPTIDASE and BENZYLOXYCARBONYL-LEUCINE-VALINE-GLYCINE-METHYLENE INHIBITOR.

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 GLYCYL ENDOPEPTIDASE P05994 (133-348) (PAPA4_CARPA)search Carica papayasearch < 90% 216 100%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P05994 (133 - 348) GLYCYL ENDOPEPTIDASE Carica papaya

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
E Papain-likesearch Cysteine proteinasessearch Papain family cysteine proteasesearch

Chain ID Molecular function (GO) Biological process (GO)
E (P05994) cysteine-type peptidase activitysearch proteolysissearch

Chain InterPro annotation
E Cysteine peptidase, cysteine active sitesearch Peptidase C1A, papain C-terminalsearch Peptidase C1A, papainsearch Cysteine peptidase, histidine active sitesearch Cysteine peptidase, asparagine active sitesearch