3pbh Summary

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REFINED CRYSTAL STRUCTURE OF HUMAN PROCATHEPSIN B AT 2.5 ANGSTROM RESOLUTION

The structure was published by Podobnik, M., Kuhelj, R., Turk, V., and Turk, D., in 1997 in a paper entitled "Crystal structure of the wild-type human procathepsin B at 2.5 A resolution reveals the native active site of a papain-like cysteine protease zymogen." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.5 Å and deposited in 1997.

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

The PDB entry contains the structure of PROCATHEPSIN B. This molecule has the UniProt identifier P07858 (CATB_HUMAN)search. The sample contained 317 residues which is < 90% of the natural sequence. Out of 317 residues 316 were observed and are deposited in the PDB.

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 PROCATHEPSIN B P07858 (10-10) (CATB_HUMAN)search ,
P07858 (81-333) (CATB_HUMAN)search
Homo sapienssearch ,
Homo sapienssearch
< 90% ,
< 90%
317 100%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P07858 (10 - 10) PROCATHEPSIN B Homo sapiens

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

Chain ID Molecular function (GO) Biological process (GO)
A (P07858) cysteine-type peptidase activitysearch cysteine-type endopeptidase activitysearch regulation of catalytic activitysearch proteolysissearch

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