4bm9 Summary

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Structure of the autoinhibited Parkin catalytic domain

The structure was published by Wauer, T. and Komander, D., in 2013 in a paper entitled "Structure of the Human Parkin Ligase Domain in an Autoinhibited State." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.25 Å and deposited in 2013.

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 329 residues which is < 90% of the natural sequence. Out of 329 residues 290 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 homohexamers.

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 (137-465) (PRKN2_HUMAN)search Homo sapienssearch < 90% 329 91%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
O60260 (137 - 465) E3 UBIQUITIN-PROTEIN LIGASE PARKIN Homo sapiens

Chain Sequence family (Pfam)
A IBR domainsearch

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

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