3p5v Summary


Actinidin from Actinidia arguta planch (Sarusashi)

The structure was published by Yogavel, M., Nithya, N., Suzuki, A., et al., Yamane, T., Velmurugan, D., and Sharma, A., in 2010 in a paper entitled "Structural analysis of actinidin and a comparison of cadmium and sulfur anomalous signals from actinidin crystals measured using in-house copper- and chromium-anode X-ray sources" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.9 Å and deposited in 2010.

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

The PDB entry contains the structure of Actinidin.

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 Actinidin A5HII2 (127-344) (A5HII2_9ERIC)search Actinidia argutasearch < 90% 220 100%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
A5HII2 (127 - 344) Actinidin Actinidia arguta

Chain Structural classification (CATH) Sequence family (Pfam)
A Cysteine proteinasessearch Papain family cysteine proteasesearch

Chain ID Molecular function (GO) Biological process (GO)
A (A5HII2) cysteine-type peptidase activitysearch proteolysissearch

Chain InterPro annotation
A Cysteine peptidase, cysteine active sitesearch Peptidase C1A, papain C-terminalsearch Peptidase C1Asearch Cysteine peptidase, histidine active sitesearch Cysteine peptidase, asparagine active sitesearch