4i1f Summary

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Structure of Parkin-S223P E3 ligase

The structure was published by Riley, B.E., Lougheed, J.C., Callaway, K., et al., Baker, J., Yednock, T., and Johnston, J.A., in 2013 in a paper entitled "Structure and function of Parkin E3 ubiquitin ligase reveals aspects of RING and HECT ligases." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.58 Å and deposited in 2012.

The experimental data on which the structure is based was also deposited.

The PDB entry contains the structure of E3 ubiquitin-protein ligase parkin. This molecule has the UniProt identifier O60260 (PRKN2_HUMAN)search. The sample contained 325 residues which is < 90% of the natural sequence. Out of 325 residues 306 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):


Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A E3 ubiquitin-protein ligase parkin O60260 (141-465) (PRKN2_HUMAN)search Homo sapienssearch < 90% 325 94%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
O60260 (141 - 465) E3 ubiquitin-protein ligase parkin Homo sapiens

Chain Sequence family (Pfam)
A IBR domainsearch

Chain ID Cellular component (GO) Molecular function (GO)
A (O60260) cytosolsearch mitochondrionsearch ubiquitin-protein transferase activitysearch zinc ion bindingsearch

Chain InterPro annotation
A Zinc finger, C6HC-typesearch E3 ubiquitin-protein ligase parkinsearch